Heme Oxygenase 1 antibody [GT664]
GTX633693
ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry
Product group Antibodies
ReactivityHuman
TargetHMOX1
Overview
- SupplierGeneTex
- Product NameHeme Oxygenase 1 antibody [GT664]
- Delivery Days Customer9
- Application Supplier NoteWB: 1:500-1:3000. ICC/IF: 1:100-1:1000. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
- ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry
- CertificationResearch Use Only
- ClonalityMonoclonal
- Clone IDGT664
- Concentration1 mg/ml
- ConjugateUnconjugated
- Gene ID3162
- Target nameHMOX1
- Target descriptionheme oxygenase 1
- Target synonymsHMOX1D, HO-1, HSP32, bK286B10, heme oxygenase 1, heat shock protein, 32-kD, heme oxygenase (decycling) 1
- HostMouse
- IsotypeIgG1
- Protein IDP09601
- Protein NameHeme oxygenase 1
- Scientific DescriptionHeme 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. [provided by RefSeq]
- ReactivityHuman
- Storage Instruction-20°C or -80°C,2°C to 8°C
- UNSPSC12352203
References
- Luo K, Stocker R, Britton WJ, et al. Haem oxygenase limits Mycobacterium marinum infection-induced detrimental ferrostatin-sensitive cell death in zebrafish. FEBS J. 2022,289(3):671-681. doi: 10.1111/febs.16209Read this paper
- Hseu YC, Vudhya Gowrisankar Y, Wang LW, et al. The in vitro and in vivo depigmenting activity of pterostilbene through induction of autophagy in melanocytes and inhibition of UVA-irradiated α-MSH in keratinocytes via Nrf2-mediated antioxidant pathways. Redox Biol. 2021,44:102007. doi: 10.1016/j.redox.2021.102007Read this paper




