Rabbit polyclonal primary
Heme Oxygenase 1 (HO-1) Rabbit Polyclonal Antibody (ER1802-73)
Synthetic peptide of n-terminal human heme oxygenase 1 (ho-1).
Mouse spleen tissue lysate, 293T, HepG2, human spleen tissue, human placenta tissue, human small intestine tissue, mouse small intestine tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified.
Heme Oxygenase 1 (HO-1)
32 kD antibody; bK286B10 antibody; D8Wsu38e antibody; heat shock protein 32 kD antibody; heat shock protein 32kD antibody; Heat shock protein antibody; Heme oxygenase (decycling) 1 antibody; Heme oxygenase 1 antibody; Hemox antibody; HMOX 1 antibody; Hmox antibody; Hmox1 antibody; HMOX1_HUMAN antibody; HO 1 antibody; HO antibody; HO-1 antibody; HO1 antibody; Hsp32 antibody
Belongs to the heme oxygenase family.
Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).
Heme oxygenases are microsomal enzymes that cleave heme to produce the antioxidant biliverdin, inorganic iron and carbon monoxide (CO). The activity of Heme Oxygenase 1 (HO-1), also designated HSP 32, is highly inducible in response to numerous stimuli, including heme, heavy metals, hormones and oxidative stress. Heme Oxygenase 2, in contrast, appears to be constituitively expressed in mammalian tissues. Heme Oxygenase 2 is involved in the production of carbon monoxide (CO) in brain, where CO is thought to act as a neurotransmitter. The CO signaling system closely parallels the signaling pathway involving nitric oxide, and regulation of the two systems is closely linked. Heme Oxygenase 3 is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis. A poor heme catalyst, Heme Oxygenase 3 has two heme regulatory motifs that may be involved in heme binding.
Wang, J., Bai, Y., Yin, S.,...
Circadian clock gene BMAL1 reduces urinary calcium oxalate stones formation by regulating NRF2/HO-1 pathway. Life sciences, 265, 118853.