Formulation: Lyophilized from sterile PBS, pH 7.4
Purity: ≥97% estimated by SDS-PAGE
Shelf life (days): 365
Notes: Histidine-rich glycoprotein is an abundant plasma glycoprotein that is involved in diverse biological processes, including angiogenesis, hemostasis, cell adhesion, and immunity.{62944,62945} It is composed of a signal peptide and two cystatin-like regions in the N-terminal domain, a central domain with a histidine-rich region (HRR) and two proline-rich regions (PRRs) on either side, and a C-terminal domain. Histidine-rich glycoprotein is mainly produced by the liver but is also found in platelets and megakaryocytes.{62946,62947} It has many binding partners, including IgG, immunoglobulin γ receptor (FcγR), and complement 1q (C1q), which bind to the N-terminal domain, zinc, heme, and microbes, which bind to the HRR, heparin and heparan sulfate, which bind to the N-terminal domain and HRR, plasminogen and thrombospondin, which bind to the N-terminal and C-terminal domains, and phospholipids, fibrinogen, and complement components, which have undefined binding regions.{62945} Histidine-rich glycoprotein is also able to bind to various cell types such as T cells, B cells, erythrocytes, endothelial cells, and several cancer types. It modulates macrophage polarization, facilitates the clearance of apoptotic and necrotic cells, promotes antitumor immunity, and has antibacterial and antiviral activities.{62944,62945} Overexpression of HRG decreases tumor burden, metastasis, hypoxia, and blood vessel density and increases tumor-associated macrophage (TAM) accumulation in several mouse xenograft models.{62948} Increased plasma levels of histidine-rich glycoprotein are associated with the development of post-thrombotic syndrome following a venous thromboembolic event (VTE).{62949} Cayman's Histidine-rich Glycoprotein (human, recombinant) protein can be used for cell-based adhesion assays. This protein consists of 518 amino acids, has a calculated molecular weight of 59 kDa, and a predicted N-terminus of Val19 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 75-80 kDa due to glycosylation.
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