The Rabbit Polyclonal anti-GALNT6 antibody has been validated for WB, ELISA and IHC. It is suitable to detect GALNT6 in samples from Human, Mouse and Dog.
GALNT6 antibody can be used for detection of GALNT6 by ELISA at 1:1562500. GALNT6 antibody can be used for detection of GALNT6 by western blot at 5.0 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000.
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Add 100 ?L of distilled water. Final antibody concentration is 1 mg/mL.
Concentration
1 mg/mL
Buffer
Antibody is lyophilized in PBS buffer with 2 % sucrose.
Handling Advice
As with any antibody avoid repeat freeze-thaw cycles.
Storage
4 °C/-20 °C
Storage Comment
For short periods of storage (days) store at 4 °C. For longer periods of storage, store GALNT6 antibody at -20 °C.
GALNT6 is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. GALNT6 is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin.This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin.