Mouse Anti-HMOX1 Recombinant Antibody (A248) (CBMAB-AP9815LY)

Mouse

Cattle, Dog, Guinea pig, Hamster, Human, Monkey, Mouse, Pig, Rabbit, Rat

A248

IgG1, κ

ICC/IF, ELISA, IHC, IP, WB

Human HO-1 synthetic peptide, amino acids 1-30

Cattle, Dog, Guinea pig, Hamster, Human, Monkey, Mouse, Pig, Rabbit, Rat

IgG1, κ

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Liquid

Affinity purity

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Heme Oxygenase 1

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. [provided by RefSeq, Jul 2008]

Heme Oxygenase 1; Heme Oxygenase (Decycling) 1; HO-1; Heat Shock Protein, 32-KD; EC 1.14.14.18; EC 1.14.99.3;

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 destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Angiogenesis Source: BHF-UCL
Cell death Source: BHF-UCL
Cellular iron ion homeostasis Source: CACAO
Cellular response to arsenic-containing substance Source: Ensembl
Cellular response to cadmium ion Source: Ensembl
Cellular response to cisplatin Source: Ensembl
Cellular response to heat Source: UniProtKB
Cellular response to hypoxia Source: UniProtKB
Cellular response to nutrient Source: Ensembl
Endothelial cell proliferation Source: BHF-UCL
Erythrocyte homeostasis Source: BHF-UCL
Excretion Source: BHF-UCL
Heme catabolic process Source: BHF-UCL
Heme oxidation Source: BHF-UCL
Intracellular signal transduction Source: BHF-UCL
Intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
Iron ion homeostasis Source: BHF-UCL
Liver regeneration Source: Ensembl
Low-density lipoprotein particle clearance Source: BHF-UCL
Negative regulation of DNA binding Source: Ensembl
Negative regulation of DNA-binding transcription factor activity Source: Ensembl
Negative regulation of epithelial cell apoptotic process Source: Ensembl
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
Negative regulation of leukocyte migration Source: BHF-UCL
Negative regulation of macroautophagy Source: Ensembl
Negative regulation of mast cell cytokine production Source: Ensembl
Negative regulation of mast cell degranulation Source: Ensembl
Negative regulation of muscle cell apoptotic process Source: Ensembl
Negative regulation of neuron apoptotic process Source: Ensembl
Negative regulation of smooth muscle cell proliferation Source: UniProtKB
Negative regulation of vascular associated smooth muscle cell proliferation Source: Ensembl
Positive regulation of angiogenesis Source: BHF-UCL
Positive regulation of apoptotic process Source: Ensembl
Positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: BHF-UCL
Positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
Positive regulation of chemokine production Source: BHF-UCL
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of macroautophagy Source: Ensembl
Positive regulation of smooth muscle cell proliferation Source: UniProtKB
Regulation of angiogenesis Source: BHF-UCL
Regulation of blood pressure Source: Ensembl
Regulation of DNA-binding transcription factor activity Source: BHF-UCL
Regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
Regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
Response to estrogen Source: Ensembl
Response to hydrogen peroxide Source: BHF-UCL
Response to nicotine Source: BHF-UCL
Response to oxidative stress Source: BHF-UCL
Response to xenobiotic stimulus Source: Ensembl
Small GTPase mediated signal transduction Source: Ensembl
Smooth muscle hyperplasia Source: BHF-UCL
Wound healing involved in inflammatory response Source: BHF-UCL

Microsome; Endoplasmic reticulum membrane

Heme oxygenase 1 deficiency (HMOX1D):
A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.