Histidine-rich glycoprotein (Hrg), mouse, recombinant

Organism: Mus musculus (Mouse). Source: Yeast. Expression Region: 19-525aa. Protein Length: Full Length of Mature Protein. Tag Info: C-terminal 6xHis-tagged. Target Protein Sequence: LSPTNCDASE PLAEKVLDLI NKGRRSGYVF ELLRVSDAHL DRAGTATVYY LALDVIESDC WVLSTKAQDD CLPSRWQSEI VIGQCKVIAT RYSNESQDLS VNGYNCTTSS VSSALRNTKD SPVLLDFFED SELYRKQARK ALDKYKTDNG DFASFRVERA ERVIRARGGE RTNYYVEFSM RNCSTQHFPR SPLVFGFCRA LLSYSIETSD LETPDSIDIN CEVFNIEDHK DTSDMKPHWG HERPLCDKHL CKLSGSRDHH HTHKTDKLGC PPPPEGKDNS DRPRLQEGAL PQLPPGYPPH SGANRTHRPS YNHSCNEHPC HGHRPHGHHP HSHHPPGHHS HGHHPHGHHP HSHHSHGHHP PGHHPHGHHP HGHHPHGHHP HGHHPHGHDF LDYGPCDPPS NSQELKGQYH RGYGPPHGHS RKRGPGKGLF PFHHQQIGYV YRLPPLNIGE VLTLPEANFP SFSLPNCNRS LQPEIQPFPQ TASRSCPGKF ESEFPQISKF FGYTPPK. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: n/a. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: 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. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Reference: n/a. Function: nan