NP_000403.1
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NCBI GenBank Nucleotide #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
59,578 Da
NCBI Official Full Name
histidine-rich glycoprotein
NCBI Official Synonym Full Names
histidine-rich glycoprotein
NCBI Protein Information
histidine-rich glycoprotein; histidine-proline-rich glycoprotein
UniProt Protein Name
Histidine-rich glycoprotein
UniProt Synonym Protein Names
Histidine-proline-rich glycoprotein; HPRG
UniProt Synonym Gene Names
UniProt Entry Name
HRG_HUMAN
NCBI Summary for HRGP
This histidine-rich glycoprotein contains two cystatin-like domains and is located in plasma and platelets. The physiological function has not been determined but it is known that the protein binds heme, dyes and divalent metal ions. It can inhibit rosette formation and interacts with heparin, thrombospondin and plasminogen. Two of the protein's effects, the inhibition of fibrinolysis and the reduction of inhibition of coagulation, indicate a potential prothrombotic effect. Mutations in this gene lead to thrombophilia due to abnormal histidine-rich glycoprotein levels. [provided by RefSeq, Jul 2008]
UniProt Comments for HRGP
HRG: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in an heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis. Defects in HRG are the cause of thrombophilia due to histidine-rich glycoprotein deficiency (THPH11). A hemostatic disorder characterized by a tendency to thrombosis.
Protein type: Secreted, signal peptide; Secreted
Chromosomal Location of Human Ortholog: 3q27
Cellular Component: plasma membrane; extracellular region
Molecular Function: serine-type endopeptidase inhibitor activity; heparan sulfate proteoglycan binding; heparin binding; protein binding; zinc ion binding; metal ion binding; heme binding; immunoglobulin binding; cysteine protease inhibitor activity; receptor binding
Biological Process: platelet activation; positive regulation of apoptosis; positive regulation of immune response to tumor cell; negative regulation of cell adhesion; chemotaxis; negative regulation of blood vessel endothelial cell migration; response to organic cyclic substance; negative regulation of cell proliferation; fibrinolysis; negative regulation of angiogenesis; platelet degranulation; negative regulation of fibrinolysis; positive regulation of focal adhesion formation; regulation of gene expression; regulation of actin cytoskeleton organization and biogenesis; regulation of blood coagulation; regulation of protein complex assembly; negative regulation of cell growth; angiogenesis; blood coagulation; regulation of peptidyl-tyrosine phosphorylation; defense response to fungus; negative regulation of cell adhesion mediated by integrin
Disease: Thrombophilia Due To Histidine-rich Glycoprotein Deficiency
Research Articles on HRGP
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Products associated with HRGP elisa kit
Pathways associated with HRGP elisa kit
Diseases associated with HRGP elisa kit
Organs/Tissues associated with HRGP elisa kit
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