127767 Results for: "Blotting"

Supplier: Bioss

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity.

Supplier: Rockland Immunochemical

Neuronal cell adhesion molecule (NrCAM) is a cell surface protein of the immunoglobulin (Ig) superfamily. NrCAM (also known as Bravo) contains six Ig domains, five fibronectin repeats, a transmembrane region and an intracellular domain. NrCAM is expressed in brain, spinal cord, peripheral nervous system and pancreas. In the spinal cord, NrCAM acts as a ligand for axonin-1 to guide commissural axons across the floor plate. NrCAM also acts as a ligand for F3 to control actin-dependent growth cone motility. NrCAM interacts with neurofascin and may facilitate the clustering of the cystoskeletal protein ankyrin G and the voltage-dependent sodium channel proteins at the node of Ranvier. NrCAM expression may play a role in the severity of certain types of tumors. NrCAM is overexpressed in high-grade astrocytomas, gliomas and glioblastoma tumor tissues. Anti-NrCam is ideal for research in Cancer and Neuroscience.
In the pancreas, NrCAM expression is upregulated in intraductal hyperplasia. Antisense NrCAM reduces the tumorigenic properties of human glioblastoma cells in vitro and slowed tumor growth in vivo. The gene encoding human NrCAM maps to chromosome 7q31.1-q31.2.

Supplier: Prosci

Ribosomes, the complexes that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPL3 is a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation.Ribosomes, the complexes that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation. This gene is co-transcribed with several small nucleolar RNA genes, which are located in several of this gene's introns. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Prosci

Cytokeratin 14 (CK14) belongs to the type I (or A or acidic) subfamily of low molecular weight keratins and exists in combination with keratin 5 (type II or B or basic). Cytokeratin 14 is found in basal cells of squamous epithelia, some glandular epithelia, myoepithelium, and mesothelial cells. antibody to cytokeratin 14 is useful in differentiating squamous cell carcinomas from poorly differentiated epithelial tumors. cytokeratin 14 antibody is one of the specific basal markers for distinguishing between basal and non-basal subtypes of breast carcinomas. Cytokeratin 14 antibody is also a good marker for differentiation of intraductal from invasive salivary duct carcinoma by the positive staining of basal cells surrounding the in-situ neoplasm as well as for differentiation of benign prostate from prostate carcinoma. Furthermore, this antibody has been useful in separating oncocytic tumors of the kidney from its renal mimics, and in identifying metaplastic carcinomas of the breast.

Supplier: Prosci

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system, causing a hyperpolarization of the membrane through the opening of a Cl− channel associated with the GABAA receptor (GABAA-R) subtype. GABAA-Rs are important therapeutic targets for a range of sedative, anxiolytic, and hypnotic agents and are implicated in several diseases including epilepsy, anxiety, depression, and sub-stance abuse. The GABAA-R is a multimeric subunit complex. To date six alphas, four betas and four gammas, plus alternative splicing variants of some of these subunits, have been identified (Olsen and Tobin, 1990; Whiting et al., 1999; Ogris et al., 2004). Injection in oocytes or mammalian cell lines of cRNA coding for alpha- and beta-subunits results in the expression of functional GABAA-Rs sensitive to GABA. However, coexpression of a gamma-subunit is required for benzodiazepine modulation. The various effects of the benzodiazepines in brain may also be mediated via different alpha-subunits of the receptor (McKernan et al., 2000; Mehta and Ticku, 1998; Ogris et al., 2004; Pöltl et al., 2003).

Supplier: Prosci

Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca2+/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca2+ transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca2+ transport and in fast-twitch muscle participates in the control of Ca2+ release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2.

Supplier: Prosci

Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila).Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle,that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein, also designated MEN)
functions as an RNA polymerase II elongation factor that increases the rateof transcription by suppressing transient pausing by RNA polymerase II. Also, ELL is thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, and has lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary.The gene encoding human ELL, which maps to chromosome 19p13.1, is one of several genes which undergo translocation with the MLL gene on chromo-some 11q23 in acute myeloid leukemia. MLL (myeloid/lymphoid leukemia,also designated ALL-1 and HRX) is a 430 kDa protein that regulates embryonal and hematopoietic development.

Supplier: Rockland Immunochemical

HbS antibodies detect the E6V mutant in the hemoglobin beta subunit. Functional adult hemoglobin (Hb) is a hetero tetramer composed of 2 alpha and 2 beta subunits (α2β2). Common isoform variants of hemoglobin include HbA, HbS, HbC, HbF, and HbA2. Hemoglobin S is the predominant hemoglobin in people with sickle cell disease. The alpha chain is normal. The disease-producing mutation exists in the beta chain, giving the molecule the structure, α2βS2. People who have one sickle mutant gene and one normal beta gene have sickle cell trait which is benign. Globin gene mutations affect the structure and expression levels of Hb. Sickle cell disease and the more benign sickle cell trait are observed in more than 100 million people globally. Perhaps the most significant mutation is the E6V in the beta subunit and the cause of SCD, but other relevant isoforms of Hb are observed. HbS antibody does not react to other forms of Hb. This antibody is ideal for investigators involved in Cardiovascular and developmental biology research.

Supplier: Proteintech

TAF15 (TAF2N or TAFII68) is a nuclear protein known to associate with a distinct subpopulation of transcription factor IID (TFIID), a multi-subunit complex that nucleates the pre-initiation complex on promoters of on protein-coding genes. TAF15 harbors a transcriptional activation domain, a RNA recognition motif and many Arg-Gly-Gly repeats that participate in RNA binding. TAF15 along with FUS and EWS constitutes the FET (FUS/EWS/TAF15) protein family of heterogeneous nuclear ribonucleoproteins (hnRNPs) class of RNA binding proteins that are multifunctional proteins implicated in numerous aspects of RNA processing/functions. TAF15 is a nuclear protein that shuttle between cytoplasm-nucleus and as RNA/ssDNA-binding protein, it play specific roles during transcription initiation at distinct promoters and enter the preinitiation complex together with the RNA polymerase II. TAF15 as well as other FET member genes are frequently translocated in sarcomas and rare hematopoietic as well as epithelial cancers. Moreover, dominant mutations in genes coding for four hnRNPs (TDP-43, FUS/TLS, TAF15, and EWS) are found in familial and sporadic cases of ALS and a chromosomal aberration involving TAF15/TAF2N is found in a form of extraskeletal myxoid chondrosarcomas (EMC).

Supplier: Bioss

Composed of more than ten subunits, the anaphase-promoting complex (APC) acts in a cell-cycle dependent manner to promote the separation of sister chromatids during the transition between metaphase and anaphase in mitosis. APC, or cyclosome, accomplishes this progression through the ubiquitination of mitotic cyclins and other regulatory proteins that are targeted for destruction during cell division. APC is phosphorylated, and thus activated, by protein kinases Cdk1/cyclin B and polo-like kinase (Plk). APC is under tight control by a number of regulatory factors, including CDC20, CDH1 and MAD2. Specifically, CDC20 and CDH1 directly bind to and activate the cyclin-ubiquitination activity of APCs. In contrast, MAD2 inhibits APC by forming a ternary complex with CDC20 and APC, thus preventing APC activation. APC10 contains a Doc1 homology domain, which is a beta-sandwich structure common to many other putative E3 ubiquitin ligases. APC10 binds to core APC subunits throughout the cell cycle. Specifically, APC10 binds to the C-terminus of CDC27/APC3. During mitosis, APC10 is localized in centrosomes and mitotic spindles. APC10 also localizes to kinetochores from prophase to anaphase, and to the midbody in telophase and cytokinesis.

Supplier: Prosci

Ribosomes, the complexes that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPL3 is a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation. Ribosomes, the complexes that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L3P family of ribosomal proteins and it is located in the cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has been suggested that the protein contributes to tat-mediated transactivation. This gene is co-transcribed with several small nucleolar RNA genes, which are located in several of this gene's introns. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Bioss

Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1.

Supplier: Bioss

Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing.

Supplier: Rockland Immunochemical

Combo Pack: This primary and secondary antibody pair comes with matched antibody pairs to detect and quantify endogenous protein levels of human AKT3. AKT3 Antibody detects AKT3 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. Anti-AKT3 Antibody is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

Supplier: Rockland Immunochemical

Combo Pack: This primary and secondary antibody pair comes with matched antibody pairs to detect and quantify endogenous protein levels of human AKT2. AKT2 Antibody detects AKT2 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. Anti-AKT2 Antibody is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

Supplier: Bioss

Neuronal orphan receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system. Transduces signals from ligands at the cell surface, through specific activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Following activation by ligand, ALK induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Acts as a receptor for ligands pleiotrophin (PTN), a secreted growth factor, and midkine (MDK), a PTN-related factor, thus participating in PTN and MDK signal transduction. PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation. MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction. Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase. Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK.

Supplier: Bioss

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.Involvement in disease; Defects in BMPR1B are the cause of acromesomelic chondrodysplasia with genital anomalies (AMDGA). Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs, and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers).Defects in BMPR1B are a cause of brachydactyly type A2 (BDA2) [MIM:112600]. Brachydactylies (BDs) are a group of inherited malformations characterized by shortening of the digits due to abnormal development of the phalanges and/or the metacarpals. They have been classified on an anatomic and genetic basis into five groups, A to E, including three subgroups (A1 to A3) that usually manifest as autosomal dominant traits. BDA2 was described first in a large Norwegian kindred. BDA2 is caused by mutations in BMPR1B gene and studies demonstrate that these mutations function as dominant negatives in vitro and in vivo.

Supplier: Rockland Immunochemical

EBI3 is a subunit in two distinct heterodimeric cytokines: interleukin-27 (IL-27) and IL-35. Like interleukin-23 (IL-23), IL-27 is a recently discovered member of the IL-6/IL-12 family of proinflammatory and immunoregulatory cytokines. It exists as a heterodimer composed of the p40-related protein EBI3 and an IL-12 p35-related protein termed p28. IL-27 is produced after activation by antigen-presenting cells and induces proliferation of naïve but not memory CD4+ T-cells. It acts by binding to its receptor WSX-1 (also known as TCCR) and gp130 which results in the activation of a Jak/STAT signaling cascade, suggesting the IL-27 is involved in the regulation of immune processes. It has been suggested that IL-27 can also be used as a therapeutic agent against cancer as it can also induce tumor-specific anti-tumor activity mediated through CD8+ T-cells, IFN-gamma, and T-bet. IL-35 is composed of EBI3 and the p35 subunit of IL-12 and has been reported to have therapeutic effects against collagen-induced arthritis by expanding the population of regulatory T cells and suppressing Th17 cells. At least two isoform of EBI3 are known to exist.

Supplier: Bioss

Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.

Supplier: Bioss

Transcriptional coactivator of the p300/CBP-mediated trancription complex. Acts as a bridge, linking TFAP2 transcription factors and the p300/CBP transcriptional coactivator complex in order to stimulate TFAP2-mediated transcriptional activation. Positively regulates TGF-beta signaling through its association with the SMAD/p300/CBP-mediated transcriptional coactivator complex. Stimulates the peroxisome proliferator-activated receptors PPARA transcriptional activity. Enhances estrogen-dependent transactivation mediated by estrogen receptors. Acts also as a transcriptional corepressor; interferes with the binding of the transcription factors HIF1A or STAT2 and the p300/CBP transcriptional coactivator complex. Participates in sex determination and early gonad development by stimulating transcription activation of SRY. Plays a role in controlling left-right patterning during embryogenesis; potentiates transcriptional activation of NODAL-mediated gene transcription in the left lateral plate mesoderm (LPM). Plays an essential role in differentiation of the adrenal cortex from the adrenogonadal primordium (AGP); stimulates WT1-mediated transcription activation thereby up-regulating the nuclear hormone receptor NR5A1 promoter activity. Associates with chromatin to the PITX2 P1 promoter region.

Supplier: Bioss

Members of the 'frizzled' gene family encode 7-transmembrane domain proteins that are receptors for Wnt signaling proteins. The Frizzled 5 protein is believed to be the receptor for the Wnt5A ligand. Frizzled 5 has been reported to be expressed in fetal kidney, fetal and adult liver, fetal lung, and adult pancreas. ESTs have been isolated from bone, liver/spleen, placenta, and prostate libraries. Frizzled 5 was cloned from a retina cDNA library. Receptor for Wnt proteins. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Coreceptor along with RYK of Wnt proteins, such as WNT1.

Supplier: Rockland Immunochemical

Neuronal cell adhesion molecule (NrCAM) is a cell surface protein of the immunoglobulin (Ig) superfamily. NrCAM (also known as Bravo) contains six Ig domains, five fibronectin repeats, a transmembrane region and an intracellular domain. NrCAM is expressed in brain, spinal cord, peripheral nervous system and pancreas. In the spinal cord, NrCAM acts as a ligand for axonin-1 to guide commissural axons across the floor plate. NrCAM also acts as a ligand for F3 to control actin-dependent growth cone motility. NrCAM interacts with neurofascin and may facilitate the clustering of the cystoskeletal protein ankyrin G and the voltage-dependent sodium channel proteins at the node of Ranvier. NrCAM expression may play a role in the severity of certain types of tumors. NrCAM is overexpressed in high-grade astrocytomas, gliomas and glioblastoma tumor tissues. Anti-NrCam is ideal for research in Cancer and Neuroscience.
In the pancreas, NrCAM expression is upregulated in intraductal hyperplasia. Antisense NrCAM reduces the tumorigenic properties of human glioblastoma cells in vitro and slowed tumor growth in vivo. The gene encoding human NrCAM maps to chromosome 7q31.1-q31.2.

Supplier: Rockland Immunochemical

Peripherin Antibody detects Peripherin. Peripherin is a ~57kDa intermediate filament subunit found initially in sensory neurons of the peripheral nervous systems, which gives the protein its name. Subsequently, peripherin was found in some sensory and other neurons of the central nervous system and also in PC12 cells. Peripherin is also expressed in certain neuroendocrine tumors and in the insulin producing cells of the pancreas. Peripherin belongs to the Class III family of intermediate filament subunits which also includes vimentin, glial fibrillary acidic protein (GFAP) and desmin. In contrast to the neurofilaments, peripherin is strongly up-regulated after nerve injury. Antibodies to peripherin can be used in identifying, classifying, and studying neurons throughout the nervous system. Peripherin is also a good diagnostic marker for ballooned axons seen in Lou Gehrig's disease (Amyotrophic lateral sclerosis) and some neuronally derived tumors. Autoantibodies to peripherin are frequently seen in the sera of patients with diabetes. Peripherin is not related to peripherin/RDS, a protein of the photoreceptor outer membrane mutations of which are causative of certain forms of slow retinal degeneration. Anti-Peripherin Antibody is ideal for investigators involved in Neuroscience and Cancer research.

Supplier: Proteintech

Cadherins are a family of transmembrane glycoproteins that mediate calcium-dependent cell-cell adhesion and play an important role in the maintenance of normal tissue architecture. E-cadherin (epithelial cadherin), also known as CDH1 (cadherin 1) or CAM 120/80, is a classical member of the cadherin superfamily which also include N-, P-, R-, and B-cadherins. It has been regarded as a marker for spermatogonial stem cells in mice. E-cadherin is expressed on the cell surface in most epithelial tissues. The extracellular region of E-cadherin establishes calcium-dependent homophilic trans binding, providing specific interaction with adjacent cells, while the cytoplasmic domain is connected to the actin cytoskeleton through the interaction with p120-, α-, β-, and γ-catenin (plakoglobin). E-cadherin is important in the maintenance of the epithelial integrity, and is involved in mechanisms regulating proliferation, differentiation, and survival of epithelial cell. E-cadherin may also play a role in tumorigenesis. It is considered to be an invasion suppressor protein and its loss is an indicator of high tumor aggressiveness. E-cadherin is sensitive to trypsin digestion in the absence of Ca2+. This polyclonal antibody recognizes 120-kDa intact E-cadherin and its 80-kDa trypsin-cleaved fragment.

Supplier: Rockland Immunochemical

The protocadherin gamma gene cluster is one of three related clusters tandemly linked on chromosome five. These gene clusters have an immunoglobulin-like organization, suggesting that a novel mechanism may be involved in their regulation and expression. The gamma gene cluster includes 22 genes divided into 3 subfamilies. Subfamily A contains 12 genes, subfamily B contains 7 genes and 2 pseudogenes, and the more distantly related subfamily C contains 3 genes.
The tandem array of 22 large, variable region exons are followed by a constant region, containing 3 exons shared by all genes in the cluster. Each variable region exon encodes the extracellular region, which includes 6 cadherin ectodomains and a transmembrane region. The constant region exons encode the common cytoplasmic region. These neural cadherin-like cell adhesion proteins most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been described for the gamma cluster genes. Anti-Protocadherin Gamma (pan) is ideal for research in Neuroscience, Cell Adhesion and Cell Signaling.

Supplier: Invitrogen

The Thermo Scientific™ Pierce™ MS-Compatible Magnetic IP Kit (Protein A/G) provides mass spectrometry-friendly reagents and an optimized protocol to enable highly effective and efficient immunoprecipitation and co-immunoprecipitation of target antigens upstream of LC-MS analysis.MS-compatible—reagents directly compatible with in-solution peptide digestion, enriched samples contain minimal detergent residuals detected using LC-MSSensitive—procedure successfully enriches low abundance proteins (low ng range)Low background—binding, wash, and elution buffers optimized to minimize enrichment of background proteinsRobust—procedure and reagents have been robustly tested with numerous targets to ensure consistent enrichment of low abundance proteins (ng range) with at least 2 peptides identified per proteinThe Pierce MS-Compatible Magnetic IP Kit (Protein A/G) uses high-quality Pierce Protein A/G Magnetic Beads to provide wider flexibility of antibody capture than either Protein A or G alone

Supplier: Prosci

H1FOO may play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. H1FOO is essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling.Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. The protein encoded is a member of the histone H1 family. This gene contains introns, unlike most histone genes. The protein encoded is a member of the histone H1 family. The related mouse gene is expressed only in oocytes.

Supplier: Bioss

Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:25537362). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation (By similarity).

Supplier: Genetex

In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. One class of stress proteins, termed the Hsp70 family, is comprised of multiple members, all of which bind ATPin vitro, but which are localized within different intracellular compartments. These include: i) Hsc70 (or constitutive form) present within the cytosol/nucleus; ii) Hsp70 (inducible form) present within the cytosol/nucleus/nucleolus; iii) the constitutive glucose-regulated 78 kDa (or BiP) protein present within the lumen of the endoplasmic reticulum; and iv) the constitutive glucose regulated 75 kDa protein present within the mitochondrial matrix. Members of the Hsp70 family are thought to function as molecular chaperones, assisting in the folding of other proteins in various intracellular compartments. Grp75 is localized in the mitochondrial matrix, where, in concert with Hsp60, is thought to participate in the re-folding of proteins translocated into this organelle. Like its E. coli homolog DnaK, Grp75 possesses a cation-dependent ATPase activity thought to be central to its function as a chaperone.

Supplier: Bioss

Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation.