CYP4A22 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q5TCH4 |
|---|---|
| Clone Names | 80311132 |
| Gene ID | 284541 |
|---|---|
| Other Names | Cytochrome P450 4A22, CYPIVA22, Fatty acid omega-hydroxylase, Lauric acid omega-hydroxylase, CYP4A22 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8785a was selected from the N-term region of human CYP4A22. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | CYP4A22 |
|---|---|
| Function | Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate and palmitate. Shows no activity towards arachidonic acid and prostaglandin A1. Lacks functional activity in the kidney and does not contribute to renal 20-hydroxyeicosatetraenoic acid (20-HETE) biosynthesis. |
| Cellular Location | Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein |

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Provided below are standard protocols that you may find useful for product applications.
Background
CYP4A22 catalyzes the omega-and (omega-1)-hydroxylation of various fatty acids such as laurate and palmitate. It shows no activity towards arachidonic acid and prostaglandin A1. This protein lacks functional activity in the kidney and does not contribute to renal 20-hydroxyeicosatetraenoic acid (20-HETE) biosynthesis.
References
Hiratsuka M., et.al., Mutat. Res. 599:98-104(2006).
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