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Anti-CYP17A1 Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P05093 |
| Host | Rabbit |
| Reactivity | Human |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Steroid 17-alpha-hydroxylase/17,20 lyase(CYP17A1) detection. Tested with WB, IHC-P in Human. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 1586 |
|---|---|
| Other Names | Steroid 17-alpha-hydroxylase/17, 20 lyase, 1.14.14.19, 17-alpha-hydroxyprogesterone aldolase, 1.14.14.32, CYPXVII, Cytochrome P450 17A1, Cytochrome P450-C17, Cytochrome P450c17, Steroid 17-alpha-monooxygenase, CYP17A1, CYP17, S17AH |
| Calculated MW | 57371 MW KDa |
| Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat Western blot, 0.1-0.5 µg/ml, Human |
| Subcellular Localization | Membrane . |
| Protein Name | Steroid 17-alpha-hydroxylase/17,20 lyase |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of human CYP17A1 (383-419aa EFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLN), different from the related mouse and rat sequences by ten amino acids. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Name | CYP17A1 {ECO:0000303|PubMed:19793597, ECO:0000312|HGNC:HGNC:2593} |
|---|---|
| Function | A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426). Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol (Probable) (PubMed:25301938, PubMed:9452426). Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:36640554, PubMed:9452426). Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA (PubMed:36640554). Also 16-alpha hydroxylates androgens, relevant for estriol synthesis (PubMed:25301938, PubMed:27339894). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:22266943, PubMed:25301938, PubMed:27339894, PubMed:9452426). |
| Cellular Location | Endoplasmic reticulum membrane. Microsome membrane |
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Provided below are standard protocols that you may find useful for product applications.
Background
Cytochrome P450 17A1, also called steroid 17α-monooxygenase, is an enzyme of the hydroxylase type that in humans is encoded by the CYP17A1 gene on chromosome 10. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. It has both 17alpha-hydroxylase and 17,20-lyase activities and is a key enzyme in the steroidogenic pathway that produces progestins, mineralocorticoids, glucocorticoids, androgens, and estrogens. Mutations in this gene are associated with isolated steroid-17 alpha-hydroxylase deficiency, 17-alpha-hydroxylase/17,20-lyase deficiency, pseudohermaphroditism, and adrenal hyperplasia.
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