Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
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. When 1 x 10 5 cells/well are added to Recombinant Mouse HPRG coated plates, adhesion is induced in a dose-dependent manner in the presence of Concanvalin A. The ED 50 for this effect is 0.6-3 μg/mL.
Source
Mouse myeloma cell line, NS0-derived Leu19-Lys525, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
AnalysisLeu19
Predicted Molecular Mass
58.5 kDa
SDS-PAGE
80-85 kDa, reducing conditions
1905-HP |
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Formulation Lyophilized from a 0.2 μm filtered solution in MES and NaCl. | ||
Reconstitution Reconstitute at 100 μg/mL in sterile PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: HPRG
Mouse histidine-rich glycoprotein (HPRG) is a multidomain, monomeric, secreted, 67 - 75 kDa member of the cystatin superfamily of molecules (1, 2). Its name derives from the fact that 22% of its amino acids (aa) are histidine and proline. In mouse, it is synthesized as a 525 amino acid (aa) precursor that contains an 18 aa signal sequence and a 507 aa mature region (3). Five distinct domains are recognized in the mature molecule. There are two N-terminal cystatin-like modules and one His-Pro-rich region that is flanked by two Pro-rich segments (3, 4). The His-Pro-rich region contains multiple tandem repeats with a GHHPH motif, while the N- and C-termini are linked by a disulfide bond (3, 5, 6). Mouse HPRG is only 60% aa identical to human HPRG, and 79% aa identical to rat 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) (1, 5). 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 (7 - 9). HPRG also shows antiangiogenic activity on endothelial cells (10). Finally, it binds to cytoplasmic ligand(s) exposed during cellular necrosis, and facilitates macrophage phagocytosis (11).
References:
Jones, A.L. et al. (2005) Immunol. Cell Biol. 83:106.
Koide, T. and S. Odani (1987) FEBS Lett. 216:17.
Hulett, M.D. and C.R. Parish (2000) Immunol. Cell Biol. 78:280.
GenBank Accession # NP_444406.
Borza, D-B. et al. (1996) Biochemistry 35:1925.
Sorensen, C.B. et al. (1993) FEBS Lett. 328:285.
Donate, F. et al. (2004) Cancer Res. 64:5812.
Borza, D-B. and W.T. Morgan (1997) J. Biol. Chem. 272:5718.
Guan, X. et al. (2004) Thromb. Haemost. 92:403.
Juarez, J.C. et al. (2002) Cancer Res. 62:5344.
Jones, A.L. et al. (2005) J. Biol. Chem. 280:35733.
Long Name:
Histidine-rich Glycoprotein Precusor
Entrez Gene IDs:
3273 (Human)
Alternate Names:
DKFZp779H1622; Histidine-proline-rich glycoprotein; histidine-rich glycoprotein; HPRG; HPRGHRGP; HRG
