Rabbit anti-Human Heme oxygenase 1 Polyclonal Antibody | anti-HMOX1 antibody

Heme oxygenase 1 polyclonal antibody

Cat. Num. AAA565226

• Gene Names: HMOX1; HO-1; HSP32; HMOX1D; bK286B10
• Reactivity: Human
• Applications: Immunohistochemistry, Western Blot
• Synonyms: Heme oxygenase 1; Polyclonal Antibody; Heme oxygenase 1 polyclonal antibody; HMOX1; Hsp32; Heat shock protein 32; HO-1; anti-HMOX1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Specificity: Recognizes human heme oxygenase 1.
• Form/Format: Liquid. Antiserum containing 10mM sodium azide.
• Sequence Length: 288

• Applicable Applications for anti-HMOX1 antibody: Immunohistochemistry (IHC), Western Blot (WB)
• Application Notes: Immunohistochemistry (1:50-1:1,000); Western Blot (1:1,000); Suggested dilutions/conditions may not be available for all applications.
• Immunogen: Synthetic peptide corresponding to aa 12-25 of human heme oxygenase 1 (HO-1) protein.
• Preparation and Storage: Long term: -20 degree C; Store unopened vial at -20 degree C until required for use. Store diluted antibody at 2-4 degree C and use within 1 month. Avoid freeze/thaw cycles.

Western Blot (WB)

(Western blot analysis: HO-1 was detected using HO-1, pAb (lanes 1, 3, 5 and 7), and HO-2 was detected using HO-2, pAb (lanes 2, 4, 6 and 8). Both antibodies were used at a dilution of 1:1000. Luminograph (ECL, 15 sec. exposure, ref. FM020/054) showing HO-1 and HO-2 expression in lysates prepared from gIFN/LPS stimulated RAW264.7 mouse macrophage cells (lanes 1 and 2), HepG2 (lanes 3 and 4), rat testis (HP9312, lanes 5 and 6) and rat spleen (HP9313, lanes 7 and 8).)

Related Product Information for anti-HMOX1 antibody

The rate limiting enzyme in heme catabolism, heme oxygenase, was first described in 1968 and was thought to be a species of cytochrome P450. However, subsequent work showed the enzyme to be a protein distinct from the P450 family and capable of catalysing the degradation of heme to biliverdin and iron, with the concomitant release of carbon monoxide. This enzyme activity is highly conserved throughout the Animal Kingdom and has been identified in algae and plants as well as in all higher species. Heme oxygenase-1 (HO-1) was first purified to homogeneity from rat liver and pig spleen and shown to have a molecular weight of 32kDa. Increased expression of HO-1 can be induced by a large number of structurally unrelated pharmacological and other agents, including cytokines and oxidants, as well as by heat shock and other forms of cellular stress. Baseline levels of HO-1 expression are high in certain tissues, including spleen and liver, but enriched enzyme preparations are recommended for experimental analysis. Recent data have demonstrated a cytoprotective role for HO-1, preventing cell death by modulating intracellular iron levels.

Product Categories/Family for anti-HMOX1 antibody

Protein Synthesis & Folding; Oxidative Stress

NCBI and Uniprot Product Information

• NCBI GI #: 123446
• NCBI GeneID: 3162
• UniProt Accession #: P09601
• Molecular Weight: 32,819 Da
• NCBI Official Full Name: Heme oxygenase 1
• NCBI Official Synonym Full Names: heme oxygenase 1
• NCBI Official Symbol: HMOX1
• NCBI Official Synonym Symbols: HO-1; HSP32; HMOX1D; bK286B10
• NCBI Protein Information: heme oxygenase 1
• UniProt Protein Name: Heme oxygenase 1
• Protein Family: Heme oxygenase
• UniProt Gene Name: HMOX1
• UniProt Synonym Gene Names: HO; HO1; HO-1
• UniProt Entry Name: HMOX1_HUMAN

NCBI 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. [provided by RefSeq, Jul 2008]

Uniprot Description

HMOX1: 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. Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family.

Protein type: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Oxidoreductase; EC 1.14.99.3

Chromosomal Location of Human Ortholog: 22q13.1

Cellular Component: caveola; cytosol; endoplasmic reticulum; endoplasmic reticulum membrane; extracellular space; membrane; nucleolus; nucleus; perinuclear region of cytoplasm

Molecular Function: enzyme binding; heme binding; heme oxygenase (decyclizing) activity; metal ion binding; phospholipase D activity; protein binding; protein homodimerization activity; signal transducer activity

Biological Process: angiogenesis; cell death; cellular iron ion homeostasis; cellular response to nutrient; DNA damage response, signal transduction resulting in induction of apoptosis; endothelial cell proliferation; erythrocyte homeostasis; excretion; healing during inflammatory response; heme catabolic process; heme oxidation; iron ion homeostasis; negative regulation of DNA binding; negative regulation of leukocyte migration; negative regulation of mast cell cytokine production; negative regulation of mast cell degranulation; negative regulation of neuron apoptosis; negative regulation of smooth muscle cell proliferation; negative regulation of transcription factor activity; porphyrin metabolic process; positive regulation of angiogenesis; positive regulation of chemokine biosynthetic process; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of smooth muscle cell proliferation; positive regulation of vasodilation; protein homooligomerization; regulation of angiogenesis; regulation of blood pressure; regulation of transcription factor activity; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; response to estrogen stimulus; response to hydrogen peroxide; response to nicotine; response to oxidative stress; small GTPase mediated signal transduction; smooth muscle hyperplasia; transmembrane transport

Disease: Heme Oxygenase 1 Deficiency; Pulmonary Disease, Chronic Obstructive