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P450R Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P16435 |
|---|---|
| Clone Names | 80808138 |
| Gene ID | 5447 |
|---|---|
| Other Names | NADPH--cytochrome P450 reductase, CPR, P450R, POR, CYPOR |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6518c was selected from the Center region of human P450R. 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 | POR {ECO:0000255|HAMAP-Rule:MF_03212} |
|---|---|
| Synonyms | CYPOR |
| Function | This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. |
| Cellular Location | Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_03212} |
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Provided below are standard protocols that you may find useful for product applications.
Background
P450R is an endoplasmic reticulum membrane oxidoreductase with an FAD-binding domain and a flavodoxin-like domain. The protein binds two cofactors, FAD and FMN, which allow it to donate electrons directly from NADPH to all microsomal P450 enzymes. Mutations in its gene have been associated with various diseases, including apparent combined P450C17 and P450C21 deficiency, amenorrhea and disordered steroidogenesis, congenital adrenal hyperplasia and Antley-Bixler syndrome.
References
Fukami,M., J. Clin. Endocrinol. Metab. 94 (5), 1723-1731 (2009)Mast,N., Arch. Biochem. Biophys. 483 (1), 81-89 (2009)Brenner,S., FEBS J. 275 (18), 4540-4557 (2008)
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