127867 Results for: "Blotting"

Supplier: Bioss

Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

Supplier: Bioss

Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

Supplier: Bioss

Acyl-coenzyme A synthetases (ACSs) are a large family of related enzymes known to catalyze the fundamental initial reaction in fatty acid metabolism. The ACS family is roughly characterized based on fatty acid chain length preference amongst different members. The nomenclature in the ACS family reflects this relationship and includes short-chain ACS (ACSS), medium-chain ACS (ACSM), long-chain ACS (ACSL) and very long-chain ACS (ACSVL). ACSVL family members are capable of activating both long (LCFAs) and very long-chain fatty acids (VLCFAs). There are six members of the human ACSVL subfamily, which have been described as solute carrier family 27A (SLC27A) gene products. They represent a group of evolutionarily conserved fatty acid transport proteins (FATPs) recognized for their role in facilitating translocation of long-chain fatty acids across the plasma membrane. The family nomenclature has recently been unified with their respective acyl-CoA synthetase family designations: ACSVL1 (FATP2), ACSVL2 (FATP6), ACSVL3 (FATP3), ACSVL4 (FATP1), ACSVL5 (FATP4) and ACSVL6 (FATP5). ACSVLs have unique expression patterns and are found in major organs of fatty acid metabolism, such as adipose tissue, liver, heart and kidney. ACSVL2 is a 619 amino acid multi-pass membrane protein. Encoded by a gene that maps to human chromosome 5q23.3, ACSVL2 may function as the predominant fatty acid protein transporter in heart.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

Hox, Pbx and Meis families of transcription factors form heteromeric complexes and bind DNA through specific homeobox domains. Hox proteins are involved in regulating tissue patterning during development, and are also expressed in lineage- and stage-specific patterns during adult hematopoietic differentiation and in leukemias. The Hox proteins, which include paralog groups 1-10, have a low intrinsic binding affinity for DNA and are instead associated into cooperative DNA binding complexes with Pbx or the Pbx- related Meis proteins, which result in an enhanced Hox-DNA binding affinity and an increased selectivity for the binding site. Both Meis1 and Meis2 (also known as Meis-related gene 1 or Mrg1) are members of the TALE (“three amino acid loop extension”) family of homeodomain-containing proteins. In addition to binding with Hox proteins, Meis1 also forms heterodimers with the ubiquitously expressed Pbx proteins, including Pbx1, Pbx2 and Pbx3, and these complexes contain distinct DNA-binding specificities. Like Hox and Pbx proteins, Meis1 is implicated in oncogenesis, as it is overexpressed as a result of adjacent retroviral insertion in BHX-2 myeloid leukemias. Two Meis-related proteins, Meis2 and Meis3 (also designated Mrg1 and Mrg2, respectively), possess largely similar sequence identity with Meis1 and are expressed in normal tissues and myeloid leukemias. In the pancreas, Meis2 preferentially associates with Pbx1, and together they associate with the pancreas-specific homeodomain factor, Pdx1, to repress Pdx1-induced transcriptional activation.

Supplier: Proteintech

The human RAB genes share structural and biochemical properties with the Ras gene superfamily. Accumulating data suggests an important role for RAB proteins either in endocytosis or in biosynthetic protein transport. The transport of newly synthesized proteins from endoplasmic reticulum to the Golgi complex and to secretory vesicles involves the movement of carrier vesicles, a process that appears to involve RAB protein function. Rab6A has been shown to be a regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Rab6B is encoded by an independent gene which is located on chromosome 3 region q21-q23. In contrast to Rab6A whose expression is ubiquitous, Rab6B is expressed in a tissue and cell-type specific manner. Rab6B is predominantly expressed in brain and the neuroblastoma cells. In brain, Rab6B was found to be specifically expressed in microglia, pericytes and Purkinje cells. Endogenous Rab6B localises to the Golgi apparatus and to ERGIC-53-positive vesicles. Comparable studies between Rab6A and Rab6B revealed distinct biochemical and cellular properties. Rab6B displays lower GTP-binding activities and is distributed over Golgi and ER membranes, whereas Rab6A is more restricted to the Golgi apparatus. Since the GTP-bound form of Rab6B does interact with all known Rab6A effectors, including Rabkinesin-6, the results suggest a cell-type specific role for Rab6B in retrograde membrane traffic at the level of the Golgi complex.

Supplier: Prosci

MCM8 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co-immunoprecipitate with MCM4, 6 and 7, which suggests that it may interact with other MCM proteins and play a role in DNA replication. Alternatively spliced transcript variants encoding distinct isoforms have been described.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co-immunoprecipitate with MCM4, 6 and 7, which suggests that it may interact with other MCM proteins and play a role in DNA replication. Alternatively spliced transcript variants encoding distinct isoforms have been described.

Supplier: Bioss

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

Supplier: Bioss

Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7.

Supplier: Bioss

The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and functions as a regulatory subunit of CDK2, whose activity is required for cell cycle G1/S transition. This protein accumulates at the G1-S phase boundary and is degraded as cells progress through S phase. Overexpression of this gene has been observed in many tumors, which results in chromosome instability, and thus may contribute to tumorigenesis. This protein was found to associate with, and be involved in, the phosphorylation of NPAT protein (nuclear protein mapped to the ATM locus), which participates in cell-cycle regulated histone gene expression and plays a critical role in promoting cell-cycle progression in the absence of pRB. Two alternatively spliced transcript variants of this gene, which encode distinct isoforms, have been described. Two additional splice variants were reported but detailed nucleotide sequence information is not yet available. Transcript Variant: This variant (1) contains a different 5' end region, which includes an upstream in-frame translation start codon, when compared to variant 2. The encoded protein has a 15 aa longer N-terminus, as compared to isoform 2.

Supplier: Prosci

CDH8 is a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. The extracellular domain consists of 5 subdomains, each containing a cadherin motif, and appears to determine the specificity of the protein's homophilic cell adhesion activity. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. This particular cadherin is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. The extracellular domain consists of 5 subdomains, each containing a cadherin motif, and appears to determine the specificity of the protein's homophilic cell adhesion activity. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. This particular cadherin is expressed in brain and is putatively involved in synaptic adhesion, axon outgrowth and guidance.

Supplier: Bioss

Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia.

Supplier: Bioss

POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

Supplier: Bioss

Hox, Pbx and Meis families of transcription factors form heteromeric complexes and bind DNA through specific homeobox domains. Hox proteins are involved in regulating tissue patterning during development, and are also expressed in lineage- and stage-specific patterns during adult hematopoietic differentiation and in leukemias. The Hox proteins, which include paralog groups 1-10, have a low intrinsic binding affinity for DNA and are instead associated into cooperative DNA binding complexes with Pbx or the Pbx- related Meis proteins, which result in an enhanced Hox-DNA binding affinity and an increased selectivity for the binding site. Both Meis1 and Meis2 (also known as Meis-related gene 1 or Mrg1) are members of the TALE (“three amino acid loop extension”) family of homeodomain-containing proteins. In addition to binding with Hox proteins, Meis1 also forms heterodimers with the ubiquitously expressed Pbx proteins, including Pbx1, Pbx2 and Pbx3, and these complexes contain distinct DNA-binding specificities. Like Hox and Pbx proteins, Meis1 is implicated in oncogenesis, as it is overexpressed as a result of adjacent retroviral insertion in BHX-2 myeloid leukemias. Two Meis-related proteins, Meis2 and Meis3 (also designated Mrg1 and Mrg2, respectively), possess largely similar sequence identity with Meis1 and are expressed in normal tissues and myeloid leukemias. In the pancreas, Meis2 preferentially associates with Pbx1, and together they associate with the pancreas-specific homeodomain factor, Pdx1, to repress Pdx1-induced transcriptional activation.

Supplier: Bioss

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 (By similarity).

Supplier: Bioss

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Supplier: Prosci

Recognizes a protein of 57kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.

Supplier: Prosci

Melanocytes produce organelles called melanosomes which produce melanin, the pigment that gives color to skin, hair, eyes, scales and feathers. gp100 was identified in an attempt to clone the gene Tyrosinase, an enzyme required for melanin synthesis. Further testing determined that gp100 is a melanoma-specific protein and is responsible for melanosome maturation, facilitating the transition from amorphous rounded vesicles to fibrillary ellipsoid organelles.
Metastatic amelanotic melanoma can often be confused with a variety of poorly differentiated carcinomas, large cell lymphomas, and sarcomas using H & E stains alone. It is also difficult to differentiate melanoma from spindle cell carcinomas and various types of mesenchymal neoplasms. Clone HMB45 gp100 antibody stains fetal and neonatal melanocytes, junctional and blue nevus cells, and malignant melanoma. It also stains angiomyolipomas, tumors most commonly associated with the kidney. Intradermal nevi, normal adult melanocytes, and non-melanocytic cells are negative. This gp100 antibody does not stain tumor cells of epithelial, lymphoid, glial, or mesenchymal origin.

Supplier: Biosensis

Coronins belong to the WD40 or WD family of proteins. Coronins appear to be particularly involved in binding to actin, actin associated proteins, tubulin and phospholipase C and have been implicated in the mechanisms of chemotaxis and phagocytosis. In mammals there are at least five major coronin proteins, named coronins 1 to 5 in one nomenclature. Another nomenclature divides these five proteins in coronins 1a and 1b, 2a, 2b and 2c (see the Human Genone Organization Gene Nomenclature Committee link for this family). The mammalian coronin family members are abundant components of eukaryotic cells and each type has a restricted cell type specific expression pattern. Coronin 1A is found exclusively in hematopoetic lineage cells such as lymphocytes, macrophages and neutrophils. This antibody is therefore an excellent marker of cells of this lineage and can also be used to study the leading edges particularly of neutrophils. Since the only hematopoetic cells found within the central nervous system are microglia, this antibody is also an excellent marker of this important cell type. Microglia are numerically fairly minor components of the nervous system, but microglial activation is seen in response to a wide variety of damage and disease states, including ALS, Alzheimer's disease and responses to brain tumors. Since coronin 1a is a constitutive component of microglia, the coronin 1a antibody can be used to study both quiescent and activated microglia.

Supplier: Prosci

This mAb recognizes a protein of ~50 kDa identified as SOX10. This mAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Prosci

CDH4 gene is a classical cadherin from the cadherin superfamily. The protein is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Based on studies in chicken and mouse, this cadherin is thought to play an important role during brain segmentation and neuronal outgrowth. In addition, a role in kidney and muscle development is indicated. Of particular interest are studies showing stable cis-heterodimers of cadherins 2 and 4 in cotransfected cell lines. Previously thought to interact in an exclusively homophilic manner, this is the first evidence of cadherin heterodimerization.This gene is a classical cadherin from the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Based on studies in chicken and mouse, this cadherin is thought to play an important role during brain segmentation and neuronal outgrowth. In addition, a role in kidney and muscle development is indicated. Of particular interest are studies showing stable cis-heterodimers of cadherins 2 and 4 in cotransfected cell lines. Previously thought to interact in an exclusively homophilic manner, this is the first evidence of cadherin heterodimerization. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is a 28S subunit protein that belongs to the ribosomal protein S15P family. The protein is more than two times the size of its E. coli counterpart, with the 12S rRNA binding sites conserved. Between human and mouse, the protein is the least conserved among small subunit ribosomal proteins.Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S15P family. The encoded protein is more than two times the size of its E. coli counterpart, with the 12S rRNA binding sites conserved. Between human and mouse, the encoded protein is the least conserved among small subunit ribosomal proteins. Pseudogenes corresponding to this gene are found on chromosomes 15q and 19q.

Supplier: Prosci

DMAP1 is a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.

Supplier: Biosensis

Nerve growth factor receptor (NGFR) is also referred to as p75(NTR) due to its molecular mass and its ability to bind at low affinity not only NGF (see 162030), but also other neurotrophins, including brain-derived neurotrophic factor (BDNF; 113505), neurotrophin-3 (NTF3; 162660), and neurotrophin-4/5 (NTF5; 162662). At the time of its discovery, NGFR was considered a unique type of protein. Subsequently, however, a large superfamily of tumor necrosis factor receptors were found to share the overall structure of NGFR (4 extracellular ligand-binding, cysteine-rich repeats, or CRs, and signaling through association with, or disassociation from, cytoplasmic interactors). The identification of this superfamily helped elucidate some of the biologic functions of NGFR, including its ultimate involvement in the nuclear factor kappa-B (NFKB; see 164011) and apoptosis pathways. As a monomer, NGFR binds NGF with low affinity. Higher affinity binding is achieved by association with higher molecular mass, low-affinity neurotrophin receptors, namely the tropomyosin receptor kinases, TRKA (NTRK1; 191315), TRKB (NTRK2; 600456), and TRKC (NTRK3; 191316). TRKA, TRKB, and TRKC are specific for or 'preferred by' NGF, NTF5 and BDNF, and NTF3, respectively. NTF3 also binds to TRKA and TRKB, but with significantly lower affinity.

Supplier: Prosci

This mAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer s disease.

Supplier: IBI Scientific

IBI Plant Isolate Total DNA Extraction Reagent System provides a quick and easy 3 step CTAB and chloroform based method to isolate Total DNA (including genomic, mitochondrial, and chloroplast DNA) from a variety of plant species (including algae and cyanobacteria)

Supplier: Bioss

c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.

Supplier: Bioss

Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier.

Supplier: Bioss

Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2.

Supplier: Prosci

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2L3 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro.This gene encodes a protein that has been identified as a component of NuRD, a nucleosome remodeling deacetylase complex identified in the nucleus of human cells. It shows a very broad expression pattern and is strongly expressed in many tissues. It may represent one member of a small gene family that encode different but related proteins involved either directly or indirectly in transcriptional regulation. Their indirect effects on transcriptional regulation may include chromatin remodeling. It is closely related to another member of this family, a protein that has been correlated with the metastatic potential of certain carcinomas. These two proteins are so closely related that they share the same types of domains. These domains include two DNA binding domains, a dimerization domain, and a domain commonly found in proteins that methylate DNA. One of the proteins known to be a target protein for this gene product is p53. Deacteylation of p53 is correlated with a loss of growth inhibition in transformed cells supporting a connection between these gene family members and metastasis.