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anti-HPRG antibody :: Rat anti-Mouse HPRG Monoclonal Antibody

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Catalog # MBS690930
Unit / Price
  0.1 mg  /  $490 +1 FREE 8GB USB
anti-HPRG antibody
Product Name

HPRG, Monoclonal Antibody

Popular Item
Also Known As

Rat Anti-Mouse HPRG

Product Synonym Names
Anti-mouse Histidine and Proline Rich Glycoprotein [HPRG] (#9G42)
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Immunogen Sequence Length
Chromosome Location
Chromosome: 16; NC_000082.6 (22951072..22961659). Location: 16 B1; 16 13.79 cM
3D Structure
ModBase 3D Structure for Q9ESB3
Clone Number
Species Reactivity
This antibody detects mouse HPRG in Western blotting.
Protein G/A affinity chromatography
This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a rat immunized with purified mouse recombinant protein of HPRG. The IgG2 fraction of the culture supernatant was purified by Protein A/G affinity chromatography.
Recombinant mouse protein of HPRG
Reconstitute the antibody with 200 ul sterile PBS and the final concentration is 500 ug/ml.
Reconstitution Buffer
PBS (sterile)
Preparation and Storage
Lyophilized samples are stable for 2 years from date of receipt when stored at -70 degree C. Reconstituted antibody can be aliquoted and stored frozen at < -20 degree C for at least for six months without detectable loss of activity.
Ships at RT or 4 degree C
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.
Other Notes
Small volumes of anti-HPRG antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
anti-HPRG antibody
Human histidine-rich glycoprotein (HPRG) is a multidomain, monomeric, secreted, 67-75 kDa member of the cystatin superfamily of molecules. Its name derives from the fact that 26% of its amino acids (aa) are histidine and proline. In human, it is synthesized as a 525 aa precursor that contains an 18 aa signal sequence and a 507 aa mature region. Five distinct domains are recognized in the mature 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. Human HPRG is only 60% aa identical to mouse HPRG. There are multiple ligands for HPRG. These include small molecular weight molecules (metal ions; heme), hemostatic molecules (heparan sulfate; TSP; plasminogen), and immune system components (T cells; macrophages). About 50% of plasma plasminogen circulates bound to HPRG. Upon immobilization to cell surface tropomyosin in a Zn ++dependent manner, it is converted to plasmin by tPA. HPRG also shows anti-angiogenic activity on vascular endothelial cells.
Applications Tested/Suitable for anti-HPRG antibody
Western Blot (WB)
Application Notes for anti-HPRG antibody
Western blot: (1:500-1000)
NCBI/Uniprot data below describe general gene information for HPRG. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
59,163 Da
NCBI Official Full Name
histidine-rich glycoprotein
NCBI Official Synonym Full Names
histidine-rich glycoprotein
NCBI Official Symbol
NCBI Official Synonym Symbols
Hprg; Hrgp; D16jh2; D18020; AI265597; AW413091
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NCBI Protein Information
histidine-rich glycoprotein; histidine-proline-rich glycoprotein
UniProt Protein Name
Histidine-rich glycoprotein
UniProt Synonym Protein Names
Histidine-proline-rich glycoprotein
UniProt Gene Name
UniProt Synonym Gene Names
UniProt Entry Name
UniProt Comments for HPRG
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. 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

By similarity. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Ref.3 Ref.5 Ref.7 Ref.8 Ref.9

Cofactor: Zinc

By similarity.

Subunit structure: Interacts with THBS1 (via the TSP type I repeats); the interaction blocks the antiangiogenic effect of THBS1 with CD36. 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 ATP5A1; 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

By similarity. Interacts with PLG (via its Kringle domains); the interaction tethers PLG to the cell surface and enhances its activation. Interacts (via the HRR domain) with TPM1; the interaction appears to contribute to the antiangiogenic properties of the HRR domain

By similarity. Interacts with THBS2; the interaction blocks the antiangiogenic effect of THBS2 with CD36. Ref.5

Subcellular location: Secreted.

Tissue specificity: Expressed in liver, blood plasma, serum and in platelets. Also present in fibrin clots, wound fluid from acute wounds and chronic leg ulcers. Ref.1 Ref.7

Domain: The His-rich (HRR) region contains approximately 12 tandem internal repeats of the 5-residue G[H/P][H/P]PH consensus sequence. HRR binds heparan sulfate and possesses antiangiogenic, antibacterial and antifungal properties through binding Candida cells, and preferentially lysing the ergosterol-containing liposomes at low pH. The tandem repeats also bind divalent metal ions and heme.The cystatin domains can also bind heparan sulfate. Binding is enhanced in the presence of zinc ions

By similarity.

Post-translational modification: Proteolytic cleavage produces several HRG fragments which are mostly disulfide-linked and, therefore, not released. Cleavage by plasmin is inhibited in the presence of heparin, zinc ions or in an acidic environment. Cleavage reduces binding of HRG to heparan sulfate, but enhances the ability of HRG to bind and tether plasminogen to the cell surface. On platelet activation, releases a 33 kDa antiangiogenic peptide which encompasses the HRR. Also cleaved in the C-terminal by plasmin

By similarity.N-glycosylated.

Disruption phenotype: Null mice are viable and fertile, but have enhanced coagulation resulting in decreased bleeding times. The observed enhanced platelet activation mediates the accelerated angiogenic switch. Also enhanced fibrinolysis. Animals are unprotected against Candida fungal infection. Also show larger tumor volume in cancerous state, an excessive stimulation of tumor angiogenesis, a suppression of tumor immune respons and an increased tumor growth and metastatic spread. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10

Sequence similarities: Contains 2 cystatin domains.

Sequence caution: The sequence AAN10183.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence AAN27996.1 differs from that shown. Reason: Erroneous gene model prediction.
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