Recombinant Human HMOX2, His-tagged

• Cat.No.: HMOX2-13856H
• Product Overview: Recombinant Human HMOX2 protein, fused to His-tag, was expressed in E.coli and purified by Ni-sepharose.

Specification

• Species: Human
• Source: E.coli
• Tag: His
• Protein Length: 1-293a.a.
• Description: Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. Alternative splice variants encoding the same protein have been identified at this locus.
• Storage: The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles.
• Storage Buffer: 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 300mM Imidazole and 0.7% Sarcosyl, 15%glycerol.

Gene Information

• Gene Name: HMOX2 heme oxygenase (decycling) 2 [ Homo sapiens ]
• Official Symbol: HMOX2
• Synonyms: HMOX2; heme oxygenase (decycling) 2; heme oxygenase 2; HO 2; HO-2
• Gene ID: 3163
• mRNA Refseq: NM_001127204
• Protein Refseq: NP_001120676
• MIM: 141251
• UniProt ID: P30519
• Chromosome Location: 16p13.3
• Pathway: Heme degradation, organism-specific biosystem; Iron uptake and transport, organism-specific biosystem; Metabolism, organism-specific biosystem; Metabolism of porphyrins, organism-specific biosystem; Mineral absorption, organism-specific biosystem; Mineral absorption, conserved biosystem; Porphyrin and chlorophyll metabolism, organism-specific biosystem
• Function: electron carrier activity; heme oxygenase (decyclizing) activity; metal ion binding; oxidoreductase activity; protein binding