+ Filter
Loading...
HRG
Loading...Anti-HRG Products
- Mouse Anti-HRG Recombinant Antibody (clone 22F2) (MOB-2989z)
-
- Derivation: Mouse
- Species Reactivity: Human
- Type: Mouse IgG2
- Application: ELISA, WB, Dot, FuncS
Compare
View More Products
Can't find the products you're looking for? Try to filter in the left sidebar.Filter By Tag
More Infomation
Our customer service representatives are available 24 hours a day, from Monday to Sunday. Contact Us
For Research Use Only. Not For Clinical Use.
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.
Protein class
Disease related genes, Human disease related genes, Plasma proteins
Predicted location
Secreted
Single cell type specificity
Cell type enriched (Hepatocytes)
Immune cell specificity
Not detected in immune cells
Cell line specificity
Cell line enhanced (HL-60, RH-30, SiHa)
Interaction
Interacts (via the HRR domain) with TPM1; the interaction appears to contribute to the antiangiogenic properties of the HRR domain. Interacts with THBS2; the interaction blocks the antiangiogenic effect of THBS2 with CD36 (By similarity). Interacts with THBS1 (via the TSP type I repeats); the interaction blocks the antiangiogenic effect of THBS1 with CD3. Interacts with PLG (via its Kringle domains); the interaction tethers PLG to the cell surface and enhances its activation. Interacts with HPSE; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts (via the HRR domain) with TMP1; the interaction partially mediates the antiangiogenic properties of HRG. Interacts with kappa and lambda light chains of IgG molecules. Interacts with ATP5F1A; the interaction occurs on the surface of T-cells and alters their cell morphology in concert with CONA. Binds IgG molecules containing kappa and lambda light chains and inhibits the formation of insoluble immunoglobulin complexes. Interacts with F12; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding to HRG, inhibits factor XII autoactivation and contact-initiated coagulation.
Molecular function
Heparin-binding
More Types Infomation