Polypeptide GalNac Transferase 3/GALNT3 Antibody [Alexa Fluor® 405]

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Product Details

Summary
Applications WB, ICC/IF
Clonality
Polyclonal
Host
Sheep
Conjugate
Alexa Fluor 405

Order Details

Polypeptide GalNac Transferase 3/GALNT3 Antibody [Alexa Fluor® 405] Summary

Immunogen
Mouse myeloma cell line NS0-derived recombinant human Polypeptide GalNac Transferase 3/GALNT3
Gln38-Asp633
Accession # Q14435
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.
Isotype
IgG
Clonality
Polyclonal
Host
Sheep
Purity Statement
Antigen Affinity-purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

Packaging, Storage & Formulations

Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
Buffer
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Background

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).

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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