SRD5A1 polyclonal Antibody | BS61336

SRD5A1 polyclonal Antibody | BS61336 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human,Mouse,Rat

Application: WB

Application Range: WB: 1:500~1:1000

Background: Steroid 5α-Reductase is an important enzyme in androgen physiology because it catalyzes the conversion of testosterone into the more potent 5α-dihydro-testosterone, which mediates androgen effects on target tissues. The enzyme exists as two isoforms: type 1, which is expressed mainly in the skin; and type 2, which is expressed mainly in the prostate. In cultured human skin cells, 5α-Reductase 1 shows heterogeneity of protein, and has different levels of transcriptional and translational expression. 5α-Reductase 1 is expressed in all portions of the hair follicle, whereas 5α-Reductase 2 is expressed only in mesenchymal portions. In addition, 5α-Reductase 1 is mainly expressed in human breast carcinoma and may play a role in the in situ production and actions of the potent androgen 5α-dihydrotestosterone, including inhibition of cancer cell proliferation in hormone-dependent human breast carcinoma. The 5α-Reductase-3α-hydroxysteroid dehydrogenase complex is present in the human brain, suggesting that the complex may be involved in the synthesis of neuroactive steroids or the catabolism of neurotoxic steroids.

Storage & Stability: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Specificity: SRD5A1 polyclonal Antibody detects endogenous levels of SRD5A1 protein.

Molecular Weight: ~ 29 kDa

Note: For research use only, not for use in diagnostic procedure.

Alternative Names: 3-oxo-5-alpha-steroid 4-dehydrogenase 1 (EC:1.3.1.22) ; SR type 1; Steroid 5-alpha-reductase 1; S5AR 1; SRD5A1

Immunogen: A synthetic peptide corresponding to residues in Human SRD5A1.

Conjugate: Unconjugated

Modification: Unmodification

Purification & Purity: The Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Pathway: