Application Note
*Optimal dilutions/concentrations should be determined by the researcher.
Application |
Recommended Dilution |
1:5000-1:20000 |
1:100-1:1000 |
1:100-1:1000 |
Not tested in other applications.
Calculated MW
Positive Control
Mouse brain , A431
Predict Reactivity
Zebrafish, Xenopus laevis(>80% identity)
Form
Liquid
Buffer
0.1M Tris, 0.1M Glycine, 10% Glycerol
Preservative
0.01% Thimerosal
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
1 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
Recombinant protein encompassing a sequence within the center region of human GALNT7. The exact sequence is proprietary.
Purification
Purified by antigen-affinity chromatography.
Conjugation
Unconjugated
RRID
AB_1950335
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
polypeptide N-acetylgalactosaminyltransferase 7 , GALNAC-T7 , GalNAcT7
Cellular Localization
Golgi apparatus membrane; Single-pass type II membrane protein
Background
This gene encodes GalNAc transferase 7, a member of the GalNAc-transferase family. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. Unlike other family members, this enzyme shows exclusive specificity for partially GalNAc-glycosylated acceptor substrates and shows no activity with non-glycosylated peptides. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation. [provided by RefSeq]
Database
Research Area