127868 Results for: "Blotting"

Supplier: Bioss

The caspase family of cysteine proteases play a key role in apoptosis. Caspase 3 is the most extensively studied apoptotic protein among caspase family members. Caspase 3 is synthesized as inactive pro enzyme that is processed in cells undergoing apoptosis by self proteolysis and/or cleavage by other upstream proteases (e.g. Caspases 8, 9 and 10). The processed form of Caspase 3 consists of large (17kDa) and small (12kDa) subunits which associate to form an active enzyme. Caspase 3 is cleaved at Asp28 Ser29 and Asp175 Ser176. The active Caspase 3 proteolytically cleaves and activates other caspases (e.g. Caspases 6, 7 and 9), as well as relevant targets in the cells (e.g. PARP and DFF). Alternative splicing of this gene results in two transcript variants which encode the same protein. In immunohistochemical studies Caspase 3 expression has been shown to be widespread but not present in all cell types (e.g. commonly reported in epithelial cells of skin, renal proximal tubules and collecting ducts). Differences in the level of Caspase 3 have been reported in cells of short lived nature (eg germinal centre B cells) and those that are long lived (eg mantle zone B cells). Caspase 3 is the predominant caspase involved in the cleavage of amyloid beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease.

Supplier: Bioss

Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.

Supplier: Bioss

PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration in vivo were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.

Supplier: Bioss

The Lyl1 gene encodes a basic helix–loop–helix transcription factor involved in T-cell acute lymphoblastic leukemia. The expression of Lyl1 is at higher levels in the majority of cases of acute myeloblastic leukemia (AML) or myelodysplastic syndrome when compared to normal bone marrow. Lyl1 is highly expressed in most AML cell lines.Lyl-1, TAL1 and TAL2 are part of a family of basic helix-loop-helix (bHLH) proteins implicated in T cell acute leukemia. TAL1, also designated SCL, is a serine phosphoprotein and basic helix-loop-helix transcription factor known to regulate embryonic hematopoiesis. TAL2 is a protein involved in T cell acute lymphoblastic leukemia through a chromosomal translocation involving TAL2 and T cell receptor ∫ chain genes. TAL2 includes a helix-loop-helix protein dimerization and DNA-binding domain that is homologous to TAL1 and Lyl-1 proto-oncogenes. Lyl-1 (lymphoblastic leukemia-derived sequence 1) is a nuclear protein. Endogenous Lyl-1 exists in complex with E2å proteins. Lyl-1 and E2å protein can form heterodimeric complexes with distinctive DNA-binding properties in hematolymphoid cells. Lyl-1 is involved in a chromosomal aberration which causes a form of T cell acute lymphoblastic leukemia (T-ALL).

Supplier: Bioss

REM (Rad and Gem related GTP binding protein) is a member of the Rad/Gem/Kir subfamily of Ras-like GTPases and shares with other members of this subfamily some unusual structural features. Among these are nonconservative amino acid substitutions within guanine nucleotide binding and hydrolysis domains, unique effector domains, extended N- and C-termini, and a conserved C-terminal sequence thought to mediate membrane association but lacking a classical isoprenylation motif. REM, with a predicted molecular weight of 32.9 kDa, is most highly expressed in cardiac muscle and is expressed at more moderate levels in lung, kidney and skeletal muscle. REM is phosphorylated in vivo and has been shown to interact with several 14-3-3 isoforms. It has been reported that the GTP-bound form of a related Ras-like GTPase, GEM/kir, inhibits high-voltage activated Ca2+ channel activities by interacting directly with the ?subunit. The reduced channel activities are the result of a decreased a-subunit expression at the plasma membrane. This inhibition of L-type Ca2+ channels prevents Ca2+-triggered exocytosis in hormone-secreting cells. There are data that suggest that REM similarly regulates Ca2+ channel expression.

Supplier: Bioss

Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Supplier: Prosci

DDX42 is a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX42 is a ATP-dependent RNA helicase. DDX42 binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. It also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein.This gene encodes a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. Two transcript variants encoding the same protein have been identified for this gene.

Supplier: Bioss

ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Supplier: Bioss

ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Supplier: Bioss

ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Supplier: Bioss

Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.

Supplier: Bioss

This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth. SUBUNIT: Active NF-kappa-B is a heterodimer of an about 50 kDa DNA-binding subunit and the weak DNA-binding subunit p65. Two heterodimers might form a labile tetramer. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL.

Supplier: Bioss

ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. ErbB3 is a membrane-bound protein which has a neuregulin binding domain but not an active kinase domain. It can therefore bind this ligand but cannot convey a signal into the cell via protein phosphorylation. However it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers including prostate, bladder and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. Isoform 2 lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported but they have not been thoroughly characterized. Defects in ERBB3 are the cause of lethal congenital contracture syndrome type 2 (LCCS2); also called Israeli Bedouin multiple contracture syndrome type A. LCCS2 is an autosomal recessive neurogenic form of a neonatally lethal arthrogryposis that is associated with atrophy of the anterior horn of the spinal cord.

Supplier: Proteintech

NBN, also named as NBS, NBS1 and P95, is a component of the MRE11/RAD50/NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. Defects in NBN are the cause of Nijmegen breakage syndrome (NBS). Defects in NBN are a cause of genetic susceptibility to breast cancer (BC). Defects in NBN may be associated with aplastic anemia. Defects in NBN might play a role in the pathogenesis of childhood acute lymphoblastic leukemia (ALL). The antibody is specific to NBN.

Supplier: Bioss

Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation in breast cancer cells through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS.

Supplier: Bioss

Src (also known as pp60src) is a non receptor Tyrosine Kinase involved in signal transduction in many biological systems and implicated in the development of human tumors. There are two critical phosphorylation sites of tyrosine on Src, tyrosine 418 and tyrosine 529 (referring to human Src sequence). The tyrosine 418 is located in the catalytic domain and is one of the autophosphorylation sites. Full catalytic activity of Src requires phosphorylation of tyrosine 418. The tyrosine 529 is located near the carboxyl terminus of Src and acts as a negative regulator, in that Src is held in the inactive form through an intramolecular interaction between the SH2 domain and the carboxyl terminus when tyrosine 529 is phosphorylated by Csk. This conformation blocks phosphorylation of tyrosine 418 at the catalytic domain, thereby preventing Src activation. When tyrosine 529 is dephosphorylated, tyrosine 418 can be maximally phosphorylated and Src becomes active. Src is a proto oncogene that may play a role in the regulation of embryonic development and cell growth. Mutations in this gene could be involved in the malignant progression of colon cancer. Immunogen: Synthetic peptide (Human) derived from the region of Src that contains tyrosine 529, based on the human sequence. The sequence is conserved in mouse (tyrosine 534), chicken (tyrosine 527) and frog (tyrosine 525).

Supplier: Proteintech

SMAD2, also named as MADH2 and MADR2, belongs to the dwarfin/SMAD family, contains 1 MH1 (MAD homology 1) domain and 1 MH2 (MAD homology 2) domain. SMAD2 is a receptor-regulated SMAD(R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. This protein may act as a tumor suppressor in colorectal carcinoma. It is phosphorylated on one or several of Thr-220, Ser-245, Ser-250, and Ser-255. In response to TGF-beta, It is phosphorylated on Ser-465/467 by TGF-beta and activin type 1 receptor kinases, and then able to interact with SMURF2, recruiting other proteins, such as SNON, for degradation. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, it is phosphorylated on Ser-240 by CaMK2. It is phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. In response to TGF-beta, it is ubiquitinated by NEDD4L, which promotes its degradation. In response to TGF-beta signaling, it is acetylated on Lys-19 by coactivators, which increases transcriptional activity. This antibody is a rabbit polyclonal antibody raised against residues near the N terminus of human SMAD2.

Supplier: Prosci

GPHN is a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. In nonneuronal tissues, the protein is also required for molybdenum cofactor biosynthesis. Mutations in this gene may be associated with the neurological condition hyperplexia and also lead to molybdenum cofactor deficiency. Numerous alternatively spliced transcript variants encoding different isoforms have been described; however, the full-length nature of all transcript variants is not currently known. This gene encodes a neuronal assembly protein that anchors inhibitory neurotransmitter receptors to the postsynaptic cytoskeleton via high affinity binding to a receptor subunit domain and tubulin dimers. In nonneuronal tissues, the encoded protein is also required for molybdenum cofactor biosynthesis. Mutations in this gene may be associated with the neurological condition hyperplexia and also lead to molybdenum cofactor deficiency. Numerous alternatively spliced transcript variants encoding different isoforms have been described; however, the full-length nature of all transcript variants is not currently known.

Supplier: Prosci

The nuclear orphan receptors NR2C1 represses transcription and binds DNA as a homodimer. NR2C1 binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. NR2C1 may function as a negative modulator to suppress androgen receptor function in prostate cancer. NR2C1 may exert an important repressor in regulating ER activity in mammary glands. The nuclear orphan receptors TR2 (NR2C1) and TR4 form a heterodimer that binds to the epsilon and gamma globin promoter DR1 sites This gene encodes a nuclear hormone receptor characterized by a highly conserved DNA binding domain (DBD), a variable hinge region, and a carboxy-terminal ligand binding domain (LBD) that is typical for all members of the steroid/thyroid hormone receptor superfamily. This protein also belongs to a large family of ligand-inducible transcription factors that regulate gene expression by binding to specific DNA sequences within promoters of target genes. Multiple alternatively spliced transcript variants have been described, but the full-length nature of some of these variants has not been determined.

Supplier: Prosci

NR0B1 is a protein that contains a DNA-binding domain. The protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in its gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism.This gene encodes a protein that contains a DNA-binding domain. The encoded protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in this gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism.This gene encodes a protein that contains a DNA-binding domain. The encoded protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in this gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism. 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: Bioss

Acts as a transcriptional activator or repressor. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells (By similarity). When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters.

Supplier: Bioss

Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis.

Supplier: MP Biomedicals

Guanidine Hydrochloride is a protein denaturant and thus having an important role in molecular weight determinations.
Guanidine Hydrochloride is a strong chaotropic agent useful for the denaturation and subsequent refolding of proteins. This strong denaturant can solubilize insoluble or denatured proteins such as inclusion bodies. This can be used as the first step in refolding proteins or enzymes into their active form. Urea and dithiothreitol (DTT) may also be necessary. Guanidine HCl is used in the isolation of RNA to dissociate the nucleoprotein into its nucleic acid and protein moieties. It is an inhibitor of RNase. Highly concentrated (6 - 8 M) Guanidine HCl solutions are used to denature native globular proteins. It apparently disrupts hydrogen bonds which hold the protein in its unique structure. However, there also is evidence suggesting that guanidine hydrocholoride may disrupt hydrophobic interactions by promoting the solubility of hydrophobic residues in aqueous solutions.

Supplier: Enzo Life Sciences

The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits.

Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. 120S Proteasomes degrade only unfolded proteins in an energy-independent manner, whereas 26S proteasomes degrade native and ubiquitinylated proteins in an ATP-dependent manner. The native protein substrates are recognised by subunits, some with ATP binding sites, of the outer 19S caps of the 26S proteasome.

Supplier: Enzo Life Sciences

VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization:
a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif
b) a more divergent proline-rich central domain (which is responsible for profilin binding)
c) a conserved C-terminal EVH2 domain.

VASP is expressed in a variety of mammalian cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens.

Supplier: Prosci

Myogenin is a member of the MyoD family of myogenic basic helix-loop-helix (bHLH) transcription factors that also includes MyoD, Myf-5, and MRF4 (also known as herculinor Myf-6). MyoD family members are expressed exclusively in skeletal muscle and play a key role in activating myogenesis by binding to enhancer sequences of muscle-specific genes. The regulatory domain of MyoD is approximately 70 amino acids in length and includes both a basic DNA binding motif and a bHLH dimerization motif. MyoD family members share about 80% amino acid homology in their bHLH motifs. Anti-myogenin labels the nuclei of myoblasts in developing muscle tissue, and is expressed in tumor cell nuclei of rhabdomyosarcoma and some leiomyosarcomas. Positive nuclear staining may occur in Wilms tumor.

Supplier: Proteintech

PRKDC, also named as HYRC, HYRC1, DNPK1 and p460, belongs to the PI3/PI4-kinase family. PRKDC is a serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ), PRKDC is required for double-strand break (DSB) repair and V(D)J recombination. PRKDC must be bound to DNA to express its catalytic properties. It promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). It is required to protect and align broken ends of DNA. PRKDC may also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. It is found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. It also involved in modulation of transcription. It recognizes the substrate consensus sequence [ST]-Q. PRKDC phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. It phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, c-myc/MYC and RFA2. The antibody recognizes the C-term of PRKDC.

Supplier: Prosci

TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. The protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in its gene have been associated with Marfan Syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors.This gene is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It encodes a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein and binds TGF-beta. This receptor/ligand complex phosphorylates proteins which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in this gene have been associated with Marfan Syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Supplier: Bioss

Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1 and CDKN1A/p21(CIP1). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis.Tissue specificity: Expressed in placenta and testis, very low expression seen in skeletal muscle. Detected in all hematopoietic tissues examined, with highest expression in thymus and bone marrow. A low level detected in the spleen and lymph node, and barely detectable level in the peripheral leukocytes. RA treatment down-regulated the expression in NT2 cell.

Supplier: Prosci

HAX1 is known to associate with hematopoietic cell-specific Lyn substrate 1, a substrate of Src family tyrosine kinases. It also interacts with the product of the polycystic kidney disease 2 gene, mutations in which are associated with autosomal-dominant polycystic kidney disease, and with the F-actin-binding protein, cortactin. It was earlier thought that this gene product is mainly localized in the mitochondria, however, recent studies indicate it to be localized in the cell body. Mutations in this gene result in autosomal recessive severe congenital neutropenia, also known as Kostmann disease.The protein encoded by this gene is known to associate with hematopoietic cell-specific Lyn substrate 1, a substrate of Src family tyrosine kinases. It also interacts with the product of the polycystic kidney disease 2 gene, mutations in which are associated with autosomal-dominant polycystic kidney disease, and with the F-actin-binding protein, cortactin. It was earlier thought that this gene product is mainly localized in the mitochondria, however, recent studies indicate it to be localized in the cell body. Mutations in this gene result in autosomal recessive severe congenital neutropenia, also known as Kostmann disease. Two transcript variants encoding different isoforms have been found for this gene.