118 products were found matching "K00510"!

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Heme oxygenase 1, also called HMOX1 and HO-1, 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. HO-1 activity is...

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Heme oxygenase 1a (Hmox1a) is one of the zebrafish homologs of the mammalian heme oxygenase 1 (HMOX1), an essential enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide. In zebrafish (Danio rerio), Hmox1a plays a critical...

Protein function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and...

Protein function: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:11121422, PubMed:19556236, PubMed:7703255). Affords protection...

Zinc protoporphyrin-9 (ZnPPIX) is an endogenous metabolite formed during heme biosynthesis under conditions of iron insufficiency or impaired iron utilization. It also regulates heme catabolism through competitive inhibition of heme oxygenase, the rate-limiting enzyme in the heme degradation pathway that produces...

Heme oxygenase (HO) converts protoheme to biliverdin, which in turn is enzymatically metabolized to bilirubin (Cay-17161). While HO-2 is constitutively expressed, HO-1 can be induced by its heme substrate as well as by heavy metals, oxidizing agents, and other environmental stresses. Tin(IV) protoporphyrin IX...

Cobaltic(III) protoporphyrin IX chloride is a metalloporphyrin and an inducer of heme oxygenase-1 (HO-1) activity. Unlike other metalloporphyrins, cobaltic(III) protoporphyrin IX chloride induces activity of HO-1, the rate-limiting enzyme in heme catabolism, in vitro and in vivo. It also reduces the activity of...

Heme oxygenases (HOs) convert protoheme to biliverdin, which in turn is enzymatically metabolized to bilirubin (Cay-17161). Tin mesoporphyrin IX is a potent, competitive inhibitor of HO activity in vitro (Ki = 14 nM). It inhibits hepatic, renal, and splenic HO activity in vivo for extended periods of time. Tin...

Protein function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and...

Anti-HO-1 Antibody was purified by affinity chromatography. A BLAST analysis was used to suggest cross-reactivity with HO-1 from Human, Mouse, Rat and Dog based on 100% homology with the immunizing sequence. Cross-reactivity with HO-1 from other sources has not been determined. Oxidative stress research. Protein...

Protein function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and...

Protein function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and...