Rabbit anti-Human HMOX1 Polyclonal Antibody | anti-HMOX1 antibody

HMOX1, ID (HMOX1, HO, HO1, Heme oxygenase 1) (PE)

Cat. Num. AAA6307395

• Gene Names: HMOX1; HO-1; HSP32; HMOX1D; bK286B10
• Reactivity: Human
• Applications: Western Blot, Flow Cytometry, Functional Assay
• Purity: Purified by Protein A Affinity Chromatography.
• Synonyms: HMOX1; Polyclonal Antibody; ID (HMOX1; HO; HO1; Heme oxygenase 1) (PE); Heme oxygenase 1; anti-HMOX1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Recognizes human HMOX1.
• Purity/Purification: Purified by Protein A Affinity Chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with R-Phycoerythrin (PE).

• Applicable Applications for anti-HMOX1 antibody: Western Blot (WB), Flow Cytometry (FC/FACS), FLISA
• Application Notes: Applications are based on unconjugated antibody.
• Immunogen: KLH-conjugated synthetic peptide mapping to a fragment of residues within amino acids 177-204 in the C-terminal region of human HMOX1, UniProt Accession #NP_002124.1; P09601.
• Conjugate: PE
• Note: Preservative Free
• Special Handling: Light sensitive
• Preparation and Storage: Store product at 4 degree C in the dark. DO NOT FREEZE! Stable at 4 degree C for 12 months after receipt as an undiluted liquid. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Caution: PE conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial prior to removing the cap.

Western Blot (WB)

(Western Blot analysis of HMOX1 (arrow) usingMBS642676. 293 cell lysates (2ug/lane) either nontransfected (Lane 1) or transiently transfected (Lane 2) with the HMOX1 gene.)

Flow Cytometry (FC/FACS)

(Flow cytometric analysis of A549 cells (right histogram) using MBS642676 compared to a negative control cell (left histogram). Goat-anti-rabbit (FITC) secondary antibodies were used for the analysis.)

Related Product Information for anti-HMOX1 antibody

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.

Product Categories/Family for anti-HMOX1 antibody

Antibodies; Enzymes

References

1. Wu, M.M., et al. Toxicol. Appl. Pharmacol. 248(3):226-233(2010). 2. Bolisetty, S., et al. J. Am. Soc. Nephrol. 21(10):1702-1712(2010). 3. Bao, W., et al. PLoS ONE 5 (8), E12371 (2010). 4. Wu, M.M., et al. J. Biomed. Sci. 17, 70 (2010). 5. Wang, X., et al. PLoS ONE 5 (8), E11934 (2010).

NCBI and Uniprot Product Information

• NCBI GI #: 4504437
• NCBI GeneID: 3162
• NCBI Accession #: NP_002124.1
• NCBI GenBank Nucleotide #: NM_002133.2
• UniProt Accession #: P09601
• Molecular Weight: 32,819 Da
• NCBI Official Full Name: heme oxygenase 1
• NCBI Official Synonym Full Names: heme oxygenase (decycling) 1
• NCBI Official Symbol: HMOX1
• NCBI Official Synonym Symbols: HO-1; HSP32; HMOX1D; bK286B10
• NCBI Protein Information: heme oxygenase 1; heat shock protein, 32-kD
• UniProt Protein Name: Heme oxygenase 1
• 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: EC 1.14.99.3; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Oxidoreductase

Chromosomal Location of Human Ortholog: 22q13.1

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

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

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

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