Recombinant Human a-N-acetylgalactosaminidase Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 6717-GH

R&D Systems, part of Bio-Techne
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6717-GH-020
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Key Product Details

Source

CHO

Accession #

P17050

Conjugate

Unconjugated

Applications

Bioactivity

View all alpha-N-acetylgalactosaminidase/NAGA Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human alpha-N-acetylgalactosaminidase/NAGA protein
Leu18-Gln411, with a C-terminal 6‑His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

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

N-terminal Sequence Analysis

Leu18

Predicted Molecular Mass

46 kDa

SDS-PAGE

50-60 kDa, reducing conditions

Activity

Measured by its ability to cleave alpha-N-acetylgalactosaminyl from 4-Nitrophenyl N-acetyl-alpha -D-galactosaminide.
The specific activity is >1800 pmol/min/μg, as measured under the described condition.

Reviewed Applications

Read 1 review rated 5 using 6717-GH in the following applications:

Formulation, Preparation and Storage

6717-GH
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, Brij and Glycerol.
Shipping The product is shipped with polar packs. 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, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: alpha-N-acetylgalactosaminidase/NAGA

NAGA is a lysosomal alpha-N-acetylgalactosaminidase that cleaves non-reducing alpha-N-acetylgalactosaminyl moieties from glycoconjugates (1). Mature NAGA has 394 amino acids and is trafficked to the lysosome via the mannose-6-phosphate receptor‑mediated pathway (2). The enzyme is a retaining exoglycosidase, where both the substrate and product of the enzymatic reaction have the same anomeric configuration (3). Deficiency in NAGA results in increased urinary excretion and tissue accumulation of glycopeptides and oligosaccharides containing terminal alpha‑N‑acetylgalactosaminyl moieties (4), manifesting as Schindler’s disease, an autosomal recessive disease with neuroaxonal dystrophy and other neurological symptoms (5). The enzyme can be used to remove alpha‑N‑acetylgalactosaminyl residues present on red blood cells thus converting blood type A to blood type O (6, 7, 8).

References

  1. Wang, A.M. et al. (1990) J. Biol. Chem. 265:21859.
  2. Sweeley, C.C. et al. (1983) Arch. Biochem. Biophys. 223:158.
  3. Garman, S.C. et al. (2002) Structure. 10:425.
  4. Eng, C.M. et al. (2001) N. Engl. J. Med. 345:9.
  5. Wang, A.M. et al. (1990) J. Clin. Invest. 86:1752.
  6. Liu, Q.P. et al. (2007) Nature Biotechnol. 25:454.
  7. Calcutt, M. J. et al. (2002) FEMS Microbiol. Lett. 214:77.
  8. Zhu, A. et al. (1996) Arch. Biochem. Biophys. 327:324.

Alternate Names

alphaNacetylgalactosaminidase, NAGA

Entrez Gene IDs

4668 (Human); 17939 (Mouse); 315165 (Rat)

Gene Symbol

NAGA

UniProt

P17050

Additional alpha-N-acetylgalactosaminidase/NAGA Products

Product Documents for Recombinant Human a-N-acetylgalactosaminidase Protein, CF

Product Datasheets

Certificate of Analysis

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Product Specific Notices for Recombinant Human a-N-acetylgalactosaminidase Protein, CF

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

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