SRD5A1 Polyclonal Antibody, AbBy Fluor™ 555 Conjugated
Selected Variant
bs-11308R-BF555-01
Size: 20 µL
Product Specifications
Background
Steroid 5a-Reductase is an important enzyme in androgen physiology because it catalyzes the conversion of testosterone into the more potent 5a-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, 5a-Reductase 1 shows heterogeneity of protein, and has different levels of transcriptional and translational expression. 5a-Reductase 1 is expressed in all portions of the hair follicle, whereas 5a-Reductase 2 is expressed only in mesenchymal portions. In addition, 5a-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 5a-dihydrotestosterone, including inhibition of cancer cell proliferation in hormone-dependent human breast carcinoma. The 5a-Reductase-3a-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.
Synonyms
3-oxo-5-alpha-steroid 4-dehydrogenase 1; SR type 1; Steroid 5-alpha-reductase 1; S5AR 1; S5A1_HUMAN.
Cellular Locus
Cytoplasm, Cell membrane
Host
Rabbit
Cross Reactivity
Human
Immunogen
101-200/259
Target
SRD5A1
Clonality
Polyclonal
Isotype
IgG
Conjugation
AbBy Fluor™ 555
Source
KLH conjugated synthetic peptide derived from human SRD5A1
Applications
WB
Purification
Purified by Protein A.
Excitation Emission
553nm/568nm
Concentration
1µg/µl
Dilution
WB (1:300-5000)
Buffer
Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Modification
Unmodified
Storage Conditions
Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.
Predicted Cross Reactivity
Mouse, Rat, Dog, Horse, Chicken
Available Sizes
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