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The antibody against HRG was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 20-260 of human HRG (NP_000403.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
The antibody against HRG was raised in Rabbit using the recombinant fusion protein containing a sequence corresponding to amino acids 20-260 of human HRG (NP_000403.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
| Cat.No | ADA-01363A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | HRG |
| Target Synonyms | HPRG; HRGP; THPH11; HRG | Form | Liquid |
| Species Reactivity | Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.02% sodium azide, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Mouse pancreas | Application | ELISA, WB |
| Immunogen Description | Recombinant fusion protein containing a sequence corresponding to amino acids 20-260 of human HRG (NP_000403.1). | Target Species | Human |
|---|---|---|---|
| Uniprot ID | P04196 | Immunogen Sequence |
Uniprot Id
P04196
Target Species
Human
Target Name
HRG
Target Full Name
Histidine-rich glycoprotein
Target Function
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 a 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.
Target Involvement
Thrombophilia due to histidine-rich glycoprotein deficiency (THPH11)
Target Subcellular Location
Secreted.
Target Tissue Specificity
Expressed in macrophages and in malignant cells. Expressed by the liver and secreted in plasma (at protein level).
Target Synonyms
HRG; Histidine-rich glycoprotein; Histidine-proline-rich glycoprotein; HPRG
Target Background
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. The encoded protein also has a peptide that displays antimicrobial activity against C. albicans, E. coli, S. aureus, P. aeruginosa, and E. faecalis. 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.
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