NAGA Human

N-Acetylgalactosaminidase Alpha Human Recombinant
Cat. No.
BT21505
Source
Sf9, Baculovirus cells.
Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NAGA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 400 amino acids (18-411) and having a molecular mass of 45.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
NAGA is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Alpha-N-acetylgalactosaminidase (NAGA) is a lysosomal exoglycosidase responsible for removing terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. This enzyme plays a crucial role in the degradation of glycolipids.
Description
Recombinant human NAGA, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It consists of 400 amino acids (residues 18-411), resulting in a molecular mass of 45.5 kDa. However, on SDS-PAGE analysis, the apparent molecular size ranges from 40 to 57 kDa. The protein incorporates a C-terminal 6-amino acid His-tag and undergoes purification via proprietary chromatographic methods.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
This formulation contains NAGA protein at a concentration of 0.5 mg/ml. The protein is dissolved in a solution of phosphate-buffered saline (pH 7.4) supplemented with 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product should be kept refrigerated at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. It is important to avoid repeated cycles of freezing and thawing.
Purity
The purity of this product exceeds 90.0% as determined by SDS-PAGE analysis.
Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
LDNGLLQTPP MGWLAWERFR CNINCDEDPK NCISEQLFME MADRMAQDGW RDMGYTYLNI DDCWIGGRDA SGRLMPDPKR FPHGIPFLAD YVHSLGLKLG IYADMGNFTC MGYPGTTLDK VVQDAQTFAE WKVDMLKLDG CFSTPEERAQ GYPKMAAALN ATGRPIAFSC SWPAYEGGLP PRVNYSLLAD ICNLWRNYDD IQDSWWSVLS ILNWFVEHQD ILQPVAGPGH WNDPDMLLIG NFGLSLEQSR AQMALWTVLA APLLMSTDLR TISAQNMDIL QNPLMIKINQ DPLGIQGRRI HKEKSLIEVY MRPLSNKASA LVFFSCRTDM PYRYHSSLGQ LNFTGSVIYE AQDVYSGDII SGLRDETNFT VIINPSGVVM WYLYPIKNLE MSQQHHHHHH.

Product Science Overview

Structure and Function

NAGA is a protein composed of 394 amino acids and is trafficked to the lysosome via the mannose-6-phosphate receptor-mediated pathway . The enzyme’s activity is measured by its ability to cleave alpha-N-acetylgalactosaminyl from substrates like 4-Nitrophenyl N-acetyl-alpha-D-galactosaminide . The specific activity of the recombinant form is greater than 1800 pmol/min/μg .

Production and Purity

The recombinant human NAGA protein is typically produced using Chinese Hamster Ovary (CHO) cell lines . The protein is purified to over 95% purity, as determined by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining . The endotoxin level is maintained below 1.0 EU per 1 μg of the protein by the LAL method .

Clinical Significance

Mutations in the NAGA gene have been identified as the cause of Schindler disease types I and II (type II also known as Kanzaki disease) . These are rare lysosomal storage disorders characterized by the accumulation of glycoconjugates in various tissues, leading to a range of clinical symptoms.

Applications

Recombinant NAGA is used in various research applications, including:

  • Biochemical assays: To study the enzyme’s activity and kinetics.
  • Disease modeling: To understand the pathophysiology of lysosomal storage disorders.
  • Therapeutic development: As a potential therapeutic agent for treating diseases caused by NAGA deficiency.
Storage and Stability

The recombinant protein is supplied as a 0.2 μm filtered solution in Tris, NaCl, Brij, and Glycerol . It is recommended to store the protein at -20 to -70 °C to maintain its stability and avoid repeated freeze-thaw cycles .

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