Human Polypeptide GalNAc Transferase 3/GALNT3 Alexa Fluor® 647-conjugated Antibody

Catalog #: AF7174R Datasheet
Catalog # Availability Size / Price Qty
AF7174R-100UG
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Human Polypeptide GalNAc Transferase 3/GALNT3 Alexa Fluor® 647-conjugated Antibody Summary

Species Reactivity
Human
Specificity
Detects human Polypeptide GalNac Transferase 3/GALNT3 in direct ELISAs and Western blots. In direct ELISAs, less than 1% cross-reactivity with recombinant human (rh) GALNT1 and rhGALNT4 is observed.
Source
Polyclonal Sheep IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Polypeptide GalNac Transferase 3/GALNT3
Gln38-Asp633
Accession # Q14435
Formulation
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide
Label
Alexa Fluor 647 (Excitation= 650 nm, Emission= 668 nm)

Applications

Recommended Concentration
Sample
Western Blot
Optimal dilution of this antibody should be experimentally determined.
 
Immunocytochemistry
Optimal dilution of this antibody should be experimentally determined.
 

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

Background: Polypeptide GalNAc Transferase 3/GALNT3

O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane‑bound proteins. Polypeptide N‑acetylgalactosaminyltransferases (GALNTs) calalyze the initial step for O-glycosylation by transferring GalNAc to Thr or Ser residues (GalNAc alpha 1-O-Ser/Thr) in the Golgi compartment. Structurally, the GALNTs consist of an N-terminal catalytic domain tethered by a short linker to a C-terminal ricin-like lectin domain containing three potential carbohydrate-binding sites (1, 2). Twenty distinct GALNT isoforms have been detected in humans. These isoforms display both unique and overlapping substrate specificities (3, 4, 5) with no known universal consensus glycosylation sequence. Glycosylation of mucins results from the successive, often hierarchical, action of several specific GALNTs (6). Expression of GALNT3 appears to be highly regulated and mainly found in pancreas and testis (7). Using a peptide library screening approach, GALNT3 was classified as an intermediate transferase that increases the density of O-linked glycans within the mucin domain following glycosylation with early transferases (5). The enzymatic activity of recombinant human GALNT3 was determined using a phosphatase‑coupled assay (8).

Long Name
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Entrez Gene IDs
2591 (Human); 144251 (Mouse); 366061 (Rat)
Alternate Names
EC 2.4.1.41; GalNAc transferase 3; GalNAc-T3; GalNAc-T3DKFZp686C10199; GALNT3; HFTC; HFTCMGC61909; HHS; HHSPolypeptide GalNAc transferase 3; polypeptide GalNAc-transferase T3; polypeptide N-acetylgalactosaminyltransferase 3; pp-GaNTase 3; Protein-UDP acetylgalactosaminyltransferase 3; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3; UDP-N-acetyl-alpha-D-galactosamine:polypeptideN-acetylgalactosaminyltransferase 3 (GalNAc-T3)

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