NAGK Human

N-Acetylglucosamine Kinase Human Recombinant
Cat. No.
BT11641
Source
E.coli.
Synonyms
N-acetylglucosamine kinase, GNK, GlcNAc kinase, N-acetyl-D-glucosamine kinase, HSA242910, EC 2.7.1.59.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NAGK Human Recombinant produced in E. coli is a single polypeptide chain containing 367 amino acids (1-344) and having a molecular mass of 39.8kDa.
NAGK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
N-acetylglucosamine kinase (NAGK) belongs to the family of eukaryotic-type N-acetylglucosamine kinases. It plays a crucial role in the salvage pathway of amino sugar metabolism in mammals by catalyzing the phosphorylation of N-acetylglucosamine (GlcNAc) to GlcNAc 6-phosphate. GlcNAc, a vital component of complex carbohydrates, is obtained from either lysosomal degradation or dietary sources. Notably, NAGK exhibits collaborative activity with STK16 and LNX1, and also possesses ManNAc kinase activity.
Description
Recombinant NAGK, of human origin, is produced in E. coli. This single polypeptide chain consists of 367 amino acids, with amino acids 1-344 representing the NAGK sequence. Its molecular weight is 39.8kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The NAGK solution is provided at a concentration of 1mg/ml. The solution is buffered with 20mM Tris-HCl at a pH of 8.0, and contains 200mM NaCl, 2mM DTT, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the NAGK solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain product integrity, avoid subjecting the solution to repeated freeze-thaw cycles.
Purity
Purity is determined by SDS-PAGE analysis and is consistently greater than 95%.
Synonyms
N-acetylglucosamine kinase, GNK, GlcNAc kinase, N-acetyl-D-glucosamine kinase, HSA242910, EC 2.7.1.59.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAIYGG VEGGGTRSEV LLVSEDGKIL AEADGLSTNH WLIGTDKCVE RINEMVNRAK RKAGVDPLVP LRSLGLSLSG GDQEDAGRIL IEELRDRFPY LSESYLITTD AAGSIATATP DGGVVLISGT GSNCRLINPD GSESGCGGWG HMMGDEGSAY WIAHQAVKIV FDSIDNLEAA PHDIGYVKQA MFHYFQVPDR LGILTHLYRD FDKCRFAGFC RKIAEGAQQG DPLSRYIFRK AGEMLGRHIV AVLPEIDPVL FQGKIGLPIL CVGSVWKSWE LLKEGFLLAL TQGREIQAQN FFSSFTLMKL RHSSALGGAS LGARHIGHLL PMDYSANAIA FYSYTFS

Product Science Overview

Function and Pathways

NAGK is involved in both the de novo and salvage pathways of amino sugar metabolism . In the de novo pathway, GlcNAc is synthesized starting from glycolysis at fructose 6-phosphate . In the salvage pathway, NAGK reutilizes GlcNAc from nutritional sources or lysosomal degradation of oligosaccharides . The phosphorylation of GlcNAc by NAGK is the initial step in the salvage pathway, leading to the formation of GlcNAc-6-phosphate .

GlcNAc-6-phosphate can then enter various metabolic pathways:

  1. Anabolic Pathway: It leads to the formation of UDP-GlcNAc, which is a substrate for GlcNAc transferases involved in complex oligosaccharide synthesis and intracellular O-GlcNAc formation .
  2. Catabolic Pathway: It links hexosamine metabolism with the glycolytic pathway, resulting in the formation of fructose 6-phosphate .
  3. Sialic Acid Biosynthesis: It can be further metabolized to N-acetylneuraminic acid, a key component in sialic acid biosynthesis .
Importance in Human Health

NAGK is a prominent salvage enzyme in amino sugar metabolism in mammals . It has been shown to interact with other proteins such as STK16 and LNX1 and also exhibits ManNAc kinase activity . The enzyme’s activity is essential for maintaining the balance of GlcNAc levels in the body, which is crucial for various cellular functions, including glycoprotein metabolism and cartilage repair .

Recombinant NAGK

Recombinant human NAGK is produced using genetic engineering techniques to express the human NAGK gene in a host organism, such as bacteria or yeast. This allows for the production of large quantities of the enzyme for research and therapeutic purposes. Recombinant NAGK is used in various biochemical studies to understand its function and role in amino sugar metabolism .

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