Rabbit polyclonal to TPST1
Mouse, Cow, Dog
Synthetic peptide conjugated to KLH derived from within residues 50 - 150 of Human TPST1.
This antibody gave a positive signal in HeLa and HepG2 whole cell lysates as well as in the following tissue lysates: Human lung; Mouse cerebellum; Rat cerebellum.
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Preservative: 0.02% Sodium azide Constituent: PBS Note: Batches of this product that have a concentration < 1mg/ml may have BSA added as a stabilising agent. If you would like information about the formulation of a specific lot, please contact our scientific support team who will be happy to help.
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Immunogen affinity purified
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 1 µg/ml. Detects a band of approximately 50 kDa (predicted molecular weight: 42 kDa).
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.
Belongs to the protein sulfotransferase family.
Golgi apparatus membrane.
Information by UniProt
Protein tyrosine sulfotransferase 1 antibody
Protein-tyrosine sulfotransferase 1 antibody
Western blot - TPST1 antibody (ab100972)
All lanes :
Anti-TPST1 antibody (ab100972) at 1 µg/ml
Lane 1 :
Lung (Human) Tissue Lysate
Lane 2 :
Cerebellum Mouse Tissue Lysate
Lane 3 :
Cerebellum Rat Tissue Lysate
Lane 4 :
HepG2 (Human hepatocellular liver carcinoma cell line) Whole Cell Lysate
Lane 5 :
HeLa (Human epithelial carcinoma cell line) Whole Cell Lysate
Lysates/proteins at 10 µg per lane.
Secondary All lanes :
Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (
) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size:
Observed band size:
50 kDa (
why is the actual band size different from the predicted?
Additional bands at:
27 kDa, 36 kDa. We are unsure as to the identity of these extra bands.
TPST1 contains a number of potential glycosylation sites (SwissProt) which may explain its migration at a higher molecular weight than predicted.
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