SULT2A1 Polyclonal Antibody
Catalogue Numbers: BS60417-50, BS60417-100
Sizes: 50µl, 100µl
Alternative Name: Bile salt sulfotransferase; Dehydroepiandrosterone sulfotransferase; DHEA-ST; Hydroxysteroid Sulfotransferase; HST; ST2; ST2A3; Sulfotransferase 2A1; ST2A1; HST; STD
Product: Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Swiss-Prot: Q06520
Host: Rabbit
Reactivity: Human, Mouse, Rat
Applications: WB
All Applications: WB: 1:500~1:1000
Background: SULT1 sulfotransferases exhibit N-sulfating activities of carcinogenic heterocyclic amines, and are selective toward phenols, whereas SULT2 enzymes prefer hydroxysteroids and SULT3 family members are selective for N-substituted aryl and alicyclic compounds. SULT2A1 catalyzes the sulfonation of procarcinogen xenobiotics, hydroxysteroids and bile acids, and is highly expressed in adrenal and liver tissues. SULT2A1 plays a role in hepatic cholesterol homeostasis. SULT2B1 consists of two isoforms, SULT2B1a and SULT2B1b, which are transcribed from the same gene by alternative splicing of their first exons. Both isoforms are highly selective for the sulphation of 3b-hydroxysteroids such as pregnenolone, epiandrosterone, DHEA and androstenediol. SULT2B1b is expressed in prostate, skin, placenta and lung.
Purification and Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Storage and Stability: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
Specificity: SULT2A1 polyclonal antibody detects endogenous levels of SULT2A1 protein.
Bioworld Molecular Weight: ~ 36 kDa
Note: For research use only, not for use in diagnostic procedure.
Extra Notes: Western blot (WB) analysis of SULT2A1 polyclonal antibody at 1:500 dilution
Lane 1: Hela cell lysate
Lane 2: sp2/0 cell lysate
Lane 3: H9C2 cell lysate
Immunogen: A synthetic peptide corresponding to residues in Human SULT2A1.
Conjugate: Unconjugated
Modification: Unmodified