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Description:
Myelin regulatory factor: Consitutes a precursor of the transcription factor. Mediates the autocatalytic cleavage that releases the Myelin regulatory factor, N-terminal component that specifically activates transcription of central nervous system (CNS) myelin genes (PubMed:23966832). Myelin regulatory factor, C-terminal: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage. Myelin regulatory factor, N-terminal: Transcription factor that specifically activates expression of myelin genes such as MBP, MOG, MAG and PLP1 during oligodendrocyte (OL) maturation, thereby playing a central role in oligodendrocyte maturation and CNS myelination. Specifically recognizes and binds DNA sequence 5'-CTGGYAC-3' in the regulatory regions of myelin-specific genes and directly activates their expression. Not only required during oligodendrocyte differentiation but is also required on an ongoing basis for the maintenance of expression of myelin genes and for the maintenance of a mature, viable oligodendrocyte phenotype (PubMed:23966832).
Description:
May be required for normal outer mitochondrial membrane dynamics. Required for coatomer-mediated retrograde transport in certain cells. May recruit other proteins to membranes with high curvature. May promote membrane fusion.Tissue specificity: Highly expressed in heart, skeletal muscle, kidney and placenta. Detected at lower levels in brain, colon, thymus, spleen, liver, small intestine, lung and peripheral blood leukocytes.
Description:
Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis.Tissue specificity: Detected in epithelial cells from colon, esophagus and kidney (at protein level). Expression is prominent in heart, kidney, placenta and skeletal muscle.
Description:
C9 is a plasma protein synthesised in the liver and monocytes consisting of a single polypeptide chain. C9 is a part of the membrane attack complex (MAC), an important component of the immune system. The MAC forms upon complement system activation by invading pathogenic bacteria and consists of the four major complement proteins: C5b, C6, C7 and C8. These complement proteins bind to the outer surface of the plasma membrane of the invading cell. C9 binds to the membrane associated C5b-8 protein, which leads to the circular polymerization of 12-18 C9 molecules. These polymerized C9 molecules form a ring structure in the membrane. Molecules can then diffuse freely through this transmembrane channel, causing cell lysis and destruction of the invading bacterial cell.
Description:
C9 is a plasma protein synthesized in the liver and monocytes consisting of a single polypeptide chain. C9 is a part of the membrane attack complex (MAC), an important component of the immune system. The MAC forms upon complement system activation by invading pathogenic bacteria and consists of the four major complement proteins: C5b, C6, C7 and C8. These complement proteins bind to the outer surface of the plasma membrane of the invading cell. C9 binds to the membrane associated C5b-8 protein, which leads to the circular polymerization of 12-18 C9 molecules. These polymerized C9 molecules form a ring structure in the membrane. Molecules can then diffuse freely through this transmembrane channel, causing cell lysis and destruction of the invading bacterial cell.
Description:
Differentiation of myogenic cells is regulated by multiple positively and negatively acting factors. One well characterized family of helix-loop-helix (HLH) proteins known to play an important role in the regulation of muscle cell development includes Myo D, myogenin, Myf-5 and Myf-6 (also designated MRF-4 or herculin). Myo D transcription factors form heterodimers with products of a more widely expressed family of bHLH genes, the E family, which consists of at least three distinct genes: E2A, IF2 and HEB. Myo D-E heterodimers bind avidly to consensus (CANNTG) E box target sites that are functionally important elements in the upstream regulatory sequences of many muscle-specific terminal differentiation genes. Both homo- and hetero-oligomers of these proteins are able to distinguish very closely related E box proteins and are believed to play important roles in lineage specific gene expression.
Description:
This gene was first identified as one of the many genes induced by interferon. The encoded protein may play a critical role in the regulation of apoptosis. A minisatellite that consists of 26 repeats of a 12 nucleotide repeating element resembling the mammalian splice donor consensus sequence begins near the end of the second exon. Alternatively spliced transcript variants that encode different isoforms by using the two downstream repeat units as splice donor sites have been described.
Description:
This gene was first identified as one of the many genes induced by interferon. The encoded protein may play a critical role in the regulation of apoptosis. A minisatellite that consists of 26 repeats of a 12 nucleotide repeating element resembling the mammalian splice donor consensus sequence begins near the end of the second exon. Alternatively spliced transcript variants that encode different isoforms by using the two downstream repeat units as splice donor sites have been described.
Description:
Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.
Description:
Smad2 is a 58 kDa member of a family of proteins involved in cell proliferation, differentiation and development. The Smad family is divided into three subclasses: receptor-regulated Smad's, activin/TGF alpha receptor-regulated (Smad2 and 3) or BMP receptor regulated (Smad1, 5, and 8); the common partner, (Smad4) that functions via its interaction to the various Smad's; and the inhibitory Smad's, (Smad6 and Smad7). Smad2 consists of two highly conserved domains, the N terminal Mad homology (MH1) and the C-terminal Mad homology 2 (MH2) domains. The MH1 domain binds DNA and regulates nuclear import and transcription while the MH2 domain conserved among all the Smad's regulates Smad2 oligomerization and binding to cytoplasmic adaptors and transcription factors. Activated Smad2 associates with Smad4 and translocates as a complex into the nucleus, allowing its binding to DNA and transcription factors. This translocation of Smad2 (as well as Smad3) into the nucleus is a central event in TGF beta signaling. Phosphorylation of threonine 8 in the calmodulin binding region of the MH1 domain by extracellular signal regulated kinase 1(ERK 1) enhances Smad2 transcriptional activity, which is negatively regulated by calmodulin. The regulation of Smad2 phosphorylation on threonine 8 by ERK 1 and calmodulin is critical for Smad2 mediated signaling.
Description:
The RIPK5 gene encodes a dual serine/threonine and tyrosine protein kinase that is expressed in multiple tissues. Multiple alternatively spliced transcript variants have been found, but the biological validity of some variants has not been determined.
Description:
CREB3L3 is a 461 amino acid single-pass type II membrane protein that localizes to the endoplasmic reticulum (ER) and, in response to ER stress, is cleaved and translocated to the nucleus. Expressed exclusively in liver, CREB3L3 functions as a transcription factor that, during ER stress, is thought to activate genes that are involved in both the unfolded protein response and the acute phase response (APR). Additionally, CREB3L3 is underexpressed in hepatocellular carcinoma, suggesting a possible role as a tumour suppressor. CREB3L3 functions as a dimer and contains one leucine zipper domain, a KDEL-like sequence and a bZIP domain, through which it conveys its DNA binding ability. Three isoforms of CREB3L3 exist due to alternative splicing events.
UOM:
1 * 100 µl
Promotion
,BOSSBS-11239R-A680EA
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