Recombinant Human GALNTL1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7850-GT

R&D Systems, part of Bio-Techne
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7850-GT-020
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Key Product Details

Source

NS0

Accession #

Q8N428

Conjugate

Unconjugated

Applications

Enzyme Activity

View all GALNTL1 Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human GALNTL1 protein
Asp27-Thr558 with C-terminal 6-His tag

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Asp27

Predicted Molecular Mass

61 kDa

SDS-PAGE

55-61 kDa, reducing conditions

Activity

Measured by its ability to transfer GalNAc from UDP-GalNAc to peptide EA2 from AnaSpec, Inc.
The specific activity is >90 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

7850-GT
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: GALNTL1

O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane-bound proteins. Polypeptide N‑acetylgalactosaminyltransferases (GALNTs) catalyze the initial step for O-glycosylation by transferring GalNAc to Thr or Ser residues (GalNAc  alpha1‑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). GALNTL1 is active toward non-glycosylated peptides as well as some glycosylated peptides and is widely expressed in most tissues, especially high in heart, spinal cord and brain (7). Phylogenetically, GALNTL1 is closely related to GALNT2 and GALNT14 (8). The enzymatic activity of recombinant human GALNTL1 was determined using a phosphatase‑coupled assay (9).

References

  1. Gerken, T.A. et al. (2011) J. Biol. Chem. 286:14493.
  2. Ten Hagen, K.G. et al. (2003) Glycobiology 13:1R.
  3. Hagen, F.K. et al. (1997) J. Biol. Chem. 272:13843.
  4. Gerken, T.A. et al. (2006) J. Biol. Chem. 281:32403.
  5. Wandall, H.H. et al. (1997) J. Biol. Chem. 272:23503.
  6. Pratt, M.R. et al. (2004) Chem. Biol. 11:1009.
  7. Raman, J. et al. (2012) Glycobiology. 22:768.
  8. Bennett, E.P. et al. (2012) Glycobiology. 22:736.
  9. Wu, Z.L. et al. (2011) Glycobiology 21:727.

Long Name

UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like 1

Alternate Names

GalNAc-T-like protein 1, GALNACT16, GALNT16

Entrez Gene IDs

57452 (Human); 108760 (Mouse); 362760 (Rat)

Gene Symbol

GALNT16

UniProt

Q8N428 (Human)

Additional GALNTL1 Products

Product Documents for Recombinant Human GALNTL1 Protein, CF

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Product Specific Notices for Recombinant Human GALNTL1 Protein, CF

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