Category: Proteins & Peptides

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Reference: GTX89037-PEP

Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 28]

Reference: GFH16-10

Platelet-Derived Growth Factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the α-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

Reference: GTX89038-PEP

This gene encodes a member of the sialomucin protein family. The encoded protein was originally identified as an important component of glomerular podocytes. Podocytes are highly differentiated epithelial cells with interdigitating foot processes covering the outer aspect of the glomerular basement membrane. Other biological activities of the encoded protein include: binding in a membrane protein complex with Na+/H+ exchanger regulatory factor to intracellular cytoskeletal elements, playing a role in hematopoetic cell differentiation, and being expressed in vascular endothelium cells and binding to L-selectin. [provided by RefSeq, Jul 28]

Reference: GFH16-100

Platelet-Derived Growth Factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the α-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

Reference: GTX89039-PEP

The protein encoded by this gene is a multi-pass membrane protein that is localized to the golgi apparatus. It is involved in the retention of endoplasmic reticulum (ER) membrane proteins in the ER and retrieval of ER membrane proteins from the early Golgi compartment to facilitate gamma-secretase complex assembly. [provided by RefSeq, Oct 29]

Reference: GFH16-1000

Platelet-Derived Growth Factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the α-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

Reference: GTX89040-PEP

This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. In the absence of mutations, however, an acquired form of this disease can result from an autoimmune response made to type VII collagen. [provided by RefSeq, Jul 28]

Reference: GFH16AF-2

Platelet-Derived Growth Factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the α-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

Reference: GTX89042-PEP

This gene encodes a protein containing domains found in the La related protein of Drosophila melanogaster. La motif-containing proteins are thought to be RNA-binding proteins, where the La motif and adjacent amino acids fold into an RNA recognition motif. The La motif is also found in proteins unrelated to the La protein. Alternative splicing has been observed at this locus and three variants, encoding distinct isoforms, are described. Additional splice variation has been identified but the full-length nature of these transcripts has not been determined. [provided by RefSeq, Jul 28]

Reference: GFH16AF-10

Platelet-Derived Growth Factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the α-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

Reference: GTX89043-PEP

This gene encodes a member of the SFRP family that contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs act as soluble modulators of Wnt signaling. Methylation of this gene is a potential marker for the presence of colorectal cancer. [provided by RefSeq, Jul 28]

Reference: GFH16AF-100

Platelet-Derived Growth Factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-α, TGF-β and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the α-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.