Product Name: A4GNT Antibody
Species Reactivity: Human
Tested Applications: ELISA, WB
Applications: A4GNT antibody can be used for detection of A4GNT by ELISA at 1:62500. A4GNT antibody can be used for detection of A4GNT by western blot at 0.25 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 – 100,000.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 39 kDa
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human A4GNT.
Host Species: Rabbit
Purification: Antibody is purified by peptide affinity chromatography method.
Physical State: Lyophilized
CAS NO.: 1268273-90-0
Product: HSP70-IN-1
Buffer: Antibody is lyophilized in PBS buffer with 2% sucrose. Add 50 μL of distilled water. Final antibody concentration is 1 mg/mL.
Concentration: 1 mg/ml
Storage Conditions: For short periods of storage (days) store at 4˚C. For longer periods of storage, store A4GNT antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: A4GNT, MGC149493, alpha4GnT
Accession NO.: NP_057245
Protein Ino: 7705859
Official Symbol: A4GNT
Geneid: 51146
Background: A4GNT is a protein from the glycosyltransferase 32 family. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. It forms a unique glycan, GlcNAcalpha1–>4Galbeta–>R and is largely associated with the Golgi apparatus membrane.This gene encodes a protein from the glycosyltransferase 32 family. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. It forms a unique glycan, GlcNAcalpha1–>4Galbeta–>R and is largely associated with the Golgi apparatus membrane. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments.
PubMed ID:http://aac.asm.org/content/51/11/4125.abstract
