HRG (Histidine-rich glycoprotein) is a plasma glycoprotein which is distinguished by its high content of histidine and proline. HRG binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Thus, a functional binding ELISA assay was constructed to detect the association of rhHRG with heparin. Briefly, Microtiter wells were coated with OVA-conjugated-heparin. rhHRG were diluted serially in 0.01M PBS (pH 7.4). Duplicate samples of 100 μl were then transferred to the coated microtiter wells and incubated for 2h at 37ºC. Wells were washed with PBST and incubated for 1h with anti-HRG PAb, then aspirated and washed 3 times. After incubation with HRP labeled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate Solution, wells were incubated 15-25 minutes at 37ºC. Finally, add 50 μl stop solution to the wells and read at 450nm immediately. The binding activity of rhHRG with heparin was in a dose dependent manner.
Lyophilized from 20 mM Tris (pH 8.0) with 150 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.01% SKL, 5% Trehalose, Proclin300. Reconstitute with 20 mM Tris and 150 mM NaCl (pH 8.0) to a concentration of 0.1-1.0 mg/mL. Do not vortex.
For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, store at -20ºC or below. After reconstitution, keep as concentrated solution.Avoid freeze-thaw cycles.
N-terminal His-Tag; Val19~Lys525 (NP_000403.1)
< 1 EU/μg
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
histidine rich glycoprotein , HPRG , HRGP , THPH11
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. [provided by RefSeq, Nov 2014]