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bs-0675P is one synthetic peptide derived from human FGFR2. Fibroblast growth factors (FGFs) are members of a large family of structurally related polypeptides that are potent physiological regulators of growth and differentiation for a wide variety of cells of mesodermal, ectodermal and endodermal origin. Four genes encoding for high affinity cell surface FGF receptors (FGFRs) have been identified: FGFR1, FGFR2, FGFR3 and FGFR4. FGFRs are members of the tyrosine kinase family of growth fac
This gene encodes a member of the immunoglobulin gene superfamily. Expression of this cell surface protein is restricted to B cell lymphocytes. This protein is a reliable marker for pre-B cells but its expression diminishes during terminal B cell differentiation in antibody secreting plasma cells. The protein has two N-terminal extracellular Ig-like domains separated by a non-Ig-like domain, a hydrophobic transmembrane domain, and a large C-terminal cytoplasmic domain. This protein forms a com
Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of
POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the
The charged multivesicular body proteins, commonly designated CHMPs, belong to the vacuolar sorting protein family and function as chromatin-modifying proteins. CHMP1-6 are all components of ESCRT (endosomal sorting complex required for transport) I, II or III complexes. These complexes are crucial for sorting endosomal articles into multivesicular bodies (MVBs), and are also required for the formation of these bodies. CHMP2B, also known as CHMP2.5 or vacuolar protein-sorting-associated prote
Vitronectin (also known as serum spreading factor, S protein of complement or epibolin) is one of the major multifunctional cell adhesive glycoproteins in mammalian plasma and serum. It is a monomeric acidic glycoprotein detected as a mixture of 75 kD and 65 kD polypeptides. Vitronectin binds to heparin, collagen, streptococci and variety of cultured cells. It also acts as an inhibitor of the complement cascade by binding to the C5b9 complex. Vitronectin promotes cell adhesion and spreading