Heme Oxygenase 2 (HMOX2) Peptide
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Description
Heme Oxygenase 2 (HMOX2) Peptide is a synthetic peptide.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Heme Oxygenase 2 (HMOX2) |
| Host | Synthetic |
| Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
| Conjugation | Unconjugated |
| Observed MW | Sequence Fragment: Internal region: C-DQAGSTLARETLED |
| Size 1 | 100 µg |
| Form | Lyophilized Reconstitute in deionized water. |
| Tested Applications | P-ELISA |
| Buffer | Prior to lyophilization: Deionized water. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Gene ID | 3163, 15369 |
| NCBI Accession | NP_002125.3 |
| Background | Protein HMOX2 |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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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 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
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Heme Oxygenase 2 Antibody is a Rabbit Polyclonal antibody against Heme Oxygenase 2. 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 Heme Oxygenase 2 belong to the heme oxygenase family. Alternative splice variants encoding the same protein have been identified at this locus.
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