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HMOX1 Recombinant Protein

CAT: 0793-32-2442-50Size: 50 µgDry Ice: NoHazardous: No
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CAT#:0793-32-2442-50Size:50 µg
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24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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Description
Source : Escherichia Coli. HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-266) and having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques. HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.
Product Name Alternative
HO-1||HSP32||bK286B10||HMOX-1||Heme oxygenase 1||HMOX1||HO||HO1.
Purification
Greater than 95.0% as determined by SDS-PAGE.
Components
HMOX1 1 mg/mL solution containing 20mM Tris-HCl pH-8, 50mM NaCl, 0.1mM PMSF and 10% glycerol.
Storage Conditions
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) .Avoid multiple freeze-thaw cycles.
Amino Acids
MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH.

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