Human alpha ‑N‑acetylgalactosaminidase/NAGA Antibody Summary
Accession # P17050
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.
Detection of Human alpha ‑N‑acetylgalactosaminidase/NAGA by Western Blot. Western blot shows lysates of human placenta tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human a-N-acetylgalactosaminidase/NAGA Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6717) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for a-N-acetylgalactosaminidase/NAGA at approximately 45 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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).
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- Sweeley, C.C. et al. (1983) Arch. Biochem. Biophys. 223:158.
- Garman, S.C. et al. (2002) Structure. 10:425.
- Eng, C.M. et al. (2001) N. Engl. J. Med. 345:9.
- Wang, A.M. et al. (1990) J. Clin. Invest. 86:1752.
- Liu, Q.P. et al. (2007) Nature Biotechnol. 25:454.
- Calcutt, M. J. et al. (2002) FEMS Microbiol. Lett. 214:77.
- Zhu, A. et al. (1996) Arch. Biochem. Biophys. 327:324.
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