Histidine-rich glycoprotein, also known as HRG and HPRG, is a glycoprotein located in plasma and platelets and contains an unusually large amount of histidine and proline. In humans, five distinct domains are recognized in the mature HPRG molecule. There are two N-terminal cystatin-like modules (aa 19 - 254) and one His-Pro-rich region (aa 350 - 497) that is flanked by two Pro-rich segments (aa 276 - 321 and 498 - 525). The His-Pro-rich region contains 10 tandem repeats with an HHPHG motif, and the N- and C-termini are linked by a disulfide bond. The specific functions of HRG remain unclear, but it is known that the protein binds heme, dyes, and divalent metal ions. It inhibits 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. HPRG is evolutionarily, functionally, and structurally related to cleaved high molecular weight kininogen (HKa), an anti-angiogenic polypeptide that stimulates apoptosis of proliferating endothelial cells through binding to cell-surface tropomyosin. The antiangiogenic activity of the multidomain plasma protein HPRG is localized to its histidine-proline-rich (H/P) domain and has recently been shown to be mediated, at least partially, through binding to cell-surface tropomyosin in fibroblast growth factor-2-activated endothelial cells.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
100 μg | In stock | $ 378.00 | |
200 μg | 5 days | $ 644.00 | |
500 μg | 5 days | $ 1,310.00 |
Biological Information | Measured by its ability to support the adhesion of MOLT-4 human acute lymphoblastic leukemia cells. (Lamb-Wharton, R.J. and W.T. Morgen, 1993, Cell Immunol. 152: 544). Human HPRG immobilized at 1 μg/ml (100 μl/well) will induce >65% MOLT4 cell adhesion (1 x 10E5 cells/well) in the presence of 7.5 μg/ml Concanvalin A. |
Description | Histidine-rich glycoprotein, also known as HRG and HPRG, is a glycoprotein located in plasma and platelets and contains an unusually large amount of histidine and proline. In humans, five distinct domains are recognized in the mature HPRG molecule. There are two N-terminal cystatin-like modules (aa 19 - 254) and one His-Pro-rich region (aa 350 - 497) that is flanked by two Pro-rich segments (aa 276 - 321 and 498 - 525). The His-Pro-rich region contains 10 tandem repeats with an HHPHG motif, and the N- and C-termini are linked by a disulfide bond. The specific functions of HRG remain unclear, but it is known that the protein binds heme, dyes, and divalent metal ions. It inhibits 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. HPRG is evolutionarily, functionally, and structurally related to cleaved high molecular weight kininogen (HKa), an anti-angiogenic polypeptide that stimulates apoptosis of proliferating endothelial cells through binding to cell-surface tropomyosin. The antiangiogenic activity of the multidomain plasma protein HPRG is localized to its histidine-proline-rich (H/P) domain and has recently been shown to be mediated, at least partially, through binding to cell-surface tropomyosin in fibroblast growth factor-2-activated endothelial cells. |
Species | Human |
Expression System | HEK293 |
Tag | His |
Accession Number | P04196 |
Synonyms | THPH11, histidine-rich glycoprotein, HRGP, HPRG |
Construction | A DNA sequence encoding the human HPRG (NP_000403.1) (Met 1-Lys 525) with a C-terminal polyhistidine tag was expressed. |
Protein Purity |
> 97 % as determined by SDS-PAGE
|
Molecular Weight | Approxiamtely 59 kDa |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
Formulation | Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA. |
Reconstitution | A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Shipping |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
Research Background | Histidine-rich glycoprotein, also known as HRG and HPRG, is a glycoprotein located in plasma and platelets and contains an unusually large amount of histidine and proline. In humans, five distinct domains are recognized in the mature HPRG molecule. There are two N-terminal cystatin-like modules (aa 19 - 254) and one His-Pro-rich region (aa 350 - 497) that is flanked by two Pro-rich segments (aa 276 - 321 and 498 - 525). The His-Pro-rich region contains 10 tandem repeats with an HHPHG motif, and the N- and C-termini are linked by a disulfide bond. The specific functions of HRG remain unclear, but it is known that the protein binds heme, dyes, and divalent metal ions. It inhibits 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. HPRG is evolutionarily, functionally, and structurally related to cleaved high molecular weight kininogen (HKa), an anti-angiogenic polypeptide that stimulates apoptosis of proliferating endothelial cells through binding to cell-surface tropomyosin. The antiangiogenic activity of the multidomain plasma protein HPRG is localized to its histidine-proline-rich (H/P) domain and has recently been shown to be mediated, at least partially, through binding to cell-surface tropomyosin in fibroblast growth factor-2-activated endothelial cells. |
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HRG/HPRG Protein, Human, Recombinant (His) THPH11 THPH 11 histidine-rich glycoprotein THPH-11 HRGP HPRG recombinant recombinant-proteins proteins protein