NAGA protein, Alpha-N-acetylgalactosaminidase recombinant protein

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Alpha-N-acetylgalactosaminidase recombinant protein

Catalog Number: 10-288-22118F

Buy NAGA protein -

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Related Product Names:

- NAGA protein; NAGA; GALB; D22S674; Alpha-N-acetylgalactosaminidase
- EC 3.2.1.49; Alpha-galactosidase B; Alpha-N-acetylgalactosaminidase

- Gene Information - Information in yellow represents specific gene information and does not necessarily represent specific product details. For more information please contact sales@genwaybio.com.

Gene Name: NAGA	Gene Name Synonym: GALB; D22S674
Gi #: 4557781	NCBI Acc #: NP_000253.1	Swiss Prot Acc #: P17050
Length (aa): 411	Mol. Weight (Da): 46565	Chrom Location: N/A

Linear Protein Map of Expressed Protein (sequence source from above GI#)

Fusion: T7 tag at N-terminus.

Source/Host: E Coli

Purity/Purification: 95%

Crossreactivity: human

Format: 10 mM Tris, pH 8.0, 0.1% Triton X-100, 0.002% NaN3.

Storage: -70 degree C. Avoid frequent freeze and thaw.

Stability: 6-12 months at -70 degree C.

Shipping: Products may be shipped on ice pack or dry ice.

APPLICATIONS for NAGA PROTEIN:

MS, SDS: Tested

ELISA, Western Blot, Enzymatic Activity: Not Tested

TESTING: (secondary reagents and protocols )

SDS: Analysis of NAGA Recombinant Protein. 4-20% SDS gradient gel. Coomassie blue staining. ( anti-NAGA protein )

NAGA protein SDS image
NAGA

NAGA PROTEIN TARGET DESCRIPTION:

Synonym Names for NAGA protein: NAGA; GALB; D22S674; EC 3.2.1.49; Alpha-galactosidase B; Alpha-N-acetylgalactosaminidase

Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides.

Subcellular Location: Lysosome.

Disease: Defects in NAGA are the cause of Schindler disease [MIM:609241]. Schindler disease is a form of NAGA deficiency characterized by early onset neuroaxonal dystrophy and neurological signs (convulsion during fever, epilepsy, psychomotor retardation and hypotonia). NAGA deficiency is typically classified in three main phenotypes: NAGA deficiency type I (Schindler disease or Schindler disease type I) with severe manifestations; NAGA deficiency type II (Kanzazi disease or Schindler disease type II) which is mild; NAGA deficiency type III (Schindler disease type III) characterized by mild-to-moderate neurologic manifestations. NAGA deficiency results in the increased urinary excretion of glycopeptides and oligosaccharides containing alpha-N-acetylgalactosaminyl moieties. Inheritance is autosomal recessive.

Disease: Defects in NAGA are the cause of Kanzaki disease [MIM:609242]; also known as NAGA deficiency type II or Schindler disease type II. Kanzaki disease is an autosomal recessive disorder characterized by late onset, angiokeratoma corporis diffusum and mild intellectual impairment.

Miscellaneous: Alpha-galactosidase B was first found to be an isoenzyme of alpha-galactosidases, but apparently it differs from alpha-galactosidase A in substrate specificity and is alpha-N-acetylgalactosaminidase.

Similarity: Belongs to the glycosyl hydrolase 27 family [view classification].

Summary: NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. Mutations in NAGA have been identified as the cause of Schindler disease types I and II (type II also known as Kanzaki disease).

Alpha-N-acetylgalactosaminidase reacts with human.

OMIM: 104170; gene. [NCBI / EBI]
609241; phenotype. [NCBI / EBI]
609242; phenotype. [NCBI / EBI]

Products similar to NAGA protein:

IgG

Macrophage specific lectin [ER-MP23], IgG

SUGGESTED PROTEIN REAGENTS - GenWay offers reagents to facilitate your research with cell-based assays, Mass Spectrometry, standards, calibrators, Western blot, cell culture, antibiotics, microwell substrates, and more!

BACKGROUND REFERENCES for NAGA PROTEIN:

Background references for antibody target are not specific to GenWay products

[1] Kanekura,T., Sakuraba,H., Matsuzawa,F., Aikawa,S., Doi,H., Hirabayashi,Y., Yoshii,N., Fukushige,T. and Kanzaki,T.
     Three dimensional structural studies of alpha-N-acetylgalactosaminidase (alpha-NAGA) in alpha-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in alpha-NAGAs resulting in different substrate specificities and clinical phenotypes
[2] Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A., Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,, et al.
     A genome annotation-driven approach to cloning the human ORFeome
[3] Mohamad,S.B., Nagasawa,H., Uto,Y. and Hori,H., et al.
     Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation
[4] Ohta,M., Ohnishi,T., Ioannou,Y.A., Hodgson,M.E., Matsuura,F. and Desnick,R.J.
     Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides
[5] Keulemans,J.L., Reuser,A.J., Kroos,M.A., Willemsen,R., Hermans,M.M., van den Ouweland,A.M., de Jong,J.G., Wevers,R.A.,, et al.
     Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype
[6] , Wang A.M., Bishop D.F., Desnick R.J.
     Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene.
[7] , Wang A.M., Desnick R.J.
     Structural organization and complete sequence of the human alpha-N-acetylgalactosaminidase gene: homology with the alpha-galactosidase A gene provides evidence for evolution from a common ancestral gene.
[8] , Tsuji S., Yamauchi T., Hiraiwa M., Isobe T., Okuyama T., Sakimura K., Takahashi Y., Nishizawa M., Uda Y., Miyatake T., et al.
     Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B).
[9] , Yamauchi T., Hiraiwa M., Kobayashi H., Uda Y., Miyatake T., Tsuji S.
     Molecular cloning of two species of cDNAs for human alpha-N-acetylgalactosaminidase and expression in mammalian cells.
[10] , Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., et al.
     A genome annotation-driven approach to cloning the human ORFeome.

Order Confirmation: Sales order confirmations are sent out upon the receipt of all orders. Please contact GenWay if you do not receive a confirmation within 1 business day of submitting your order.

Precautions: NAGA protein is for in vitro research use only. Not for use in diagnostics or therapeutic procedures.

Important Notes: During shipment, small volumes of NAGA protein vial. For products with volumes of 200 µL or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container’s cap. Actual concentration, volume and quantity will be printed on the vial's label. Please refer to the vials label for this information.

Copyright: This GenWay TDS is copyrighted. This datasheet is produced based partially on data from Swiss-Prot/TrEMBL and NCBI. To better serve our clients with everything we know about NAGA protein, all related information, articles, resources about NAGA protein are being stored on our online database. Let us know if you have questions regarding this product.

Disclaimer: For documents and software available from this server, GenWay neither warrants nor assumes any legal liability or responsibility for the accuracy, completeness or utility of any information, product or process disclosed.

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