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Description:
Atypical chemokine receptor that controls chemokine levels and localisation 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 (internalising 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 internalisation 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.
Description:
TID1 is a human homolog of the Drosophila tumor suppressor lethal tumerous imaginal discs and encodes two mitochondrial matrix localized splice variants of human Tid1 designated hTid1S and hTid1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperons for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid1L increases apoptosis induced by DNA damaging agents as mitomycin C and TNF alpha. A J domain mutant of hTid1L can dominantly suppress apoptosis and in sharp contrast the J domain mutant of hTid1S increases apoptosis. Expression of hTid1S and hTid1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti and pro apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.
Description:
Replication factor C (RFC) is an essential DNA polymerase accessory protein that is required for numerous aspects of DNA metabolism, including DNA replication, DNA repair and telomere metabolism. RFC is a heteropentameric complex that recognizes a primer on a template DNA, binds to a primer terminus and loads proliferating cell nuclear antigen (PCNA) onto DNA at primer-template junctions in an ATP-dependent reaction. All five of the RFC subunits share a set of related sequences (RFC boxes) that include nucleotide-binding consensus sequences. Four of the five RFC genes (including RFC1, RFC2, RFC3 and RFC4) have consensus ATP-binding motifs. The small RFC proteins, RFC2, RFC3, RFC4 and RFC5, interact with Rad24, whereas the RFC1 subunit does not. RFC1 is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during FAS-mediated apoptosis. In addition, phosphorylation of the PCNA binding domain of RFC1 by Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) inhibits DNA synthesis. The human RFC1 gene maps to chromosome 4p14 and encodes the RFC1 subunit.
Description:
May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death (By similarity). May play an important role in the pathogenesis of neurogenetic diseases.Tissue specificity: Found in ovarian granulosa cells, testis, prostate and seminal vesicle tissue. High levels also detected in liver.
Description:
This gene encodes coagulation factor VIII, which participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
Description:
Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.
Description:
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Description:
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Description:
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion.
Description:
Nck is a highly conserved, oncogenic protein. It is a common target for the action of different surface receptors, encoding one SH2 and three SH3 domains, the Src homology motifs found in nonreceptor tyrosine kinases, Ras GTPase activating protein, phosphatidylinositol 3 kinase, and phospholipase Cg. Nck is widely expressed in various tissues and in cell lines from human, murine, and rat origins. Nck is phosphorylated on tyrosine, serine, and threonine residues in response to stimulation of EGF and PDGF in A431 and NIH 3T3 cells respectively. Like other SH2 containing proteins, Nck is associated with tyrosine autophosphorylated EGF or PDGF receptors via its SH2 domain. Overexpression of Nck leads to transformation of NIH 3T3 cells.
Description:
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. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis.
Description:
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. The MCM complex consisting of this protein and MCM2, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumour suppressor protein RB1/RB. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
UOM:
1 * 100 µl
Promotion
,BOSSBS-10319R-A680EA
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