UGDH Human
UDP-Glucose Dehydrogenase Human Recombinant
Cat. No.
BT15148
Source
Escherichia Coli.
Synonyms
GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% 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
UGDH Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 533 amino acids (1-494 a.a.) and having a molecular mass of 59.5 kDa. The UGDH is fused to a 39 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
UDP-glucose dehydrogenase (UGDH) is a critical enzyme involved in the biosynthesis of glycosaminoglycans, essential components of the extracellular matrix. It belongs to the UDP-glucose/GDP-mannose dehydrogenase family and is ubiquitously expressed, with a predominant presence in the liver. UGDH catalyzes the conversion of UDP-glucose to UDP-glucuronate, a key step in the formation of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These complex carbohydrates play vital roles in various cellular processes, including signal transduction, cell migration, and have implications in cancer progression.
Description
Recombinant Human UGDH, expressed in E. coli, is available as a purified, non-glycosylated polypeptide chain. This protein consists of 533 amino acids, with a sequence encompassing residues 1-494, resulting in a molecular weight of 59.5 kDa. For purification and detection purposes, a 39 amino acid His-Tag is fused to the N-terminus. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The provided solution contains 0.5mg/ml of Human UGDH in a buffer consisting of 20mM Tris-HCl (pH 8), 1mM DTT, 1mM EDTA, 0.1M NaCl, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the solution can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. To further enhance long-term stability, consider adding a carrier protein (0.1% HSA or BSA). It is crucial to avoid repeated freeze-thaw cycles to maintain protein integrity and activity.
Purity
The purity of the UGDH protein is greater than 95%, as determined by SDS-PAGE analysis.
Biological Activity
The enzyme exhibits a specific activity greater than 2500 pmol/min/µg. This activity is determined by measuring the enzyme's ability to convert UDP-glucose to UDP-glucuronate at a rate of 1.0 pmole per minute per microgram of enzyme at a pH of 8.7 and a temperature of 37°C.
Synonyms
GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM FEIKKICCIG AGYVGGPTCS VIAHMCPEIR VTVVDVNESR INAWNSPTLP IYEPGLKEVV ESCRGKNLFF STNIDDAIKE ADLVFISVNT PTKTYGMGKG RAADLKYIEA CARRIVQNSN GYKIVTEKST VPVRAAESIR RIFDANTKPN LNLQVLSNPE FLAEGTAIKD LKNPDRVLIG GDETPEGQRA VQALCAVYEH WVPREKILTT NTWSSELSKL AANAFLAQRI SSINSISALC EATGADVEEV ATAIGMDQRI GNKFLKASVG FGGSCFQKDV LNLVYLCEAL NLPEVARYWQ QVIDMNDYQR RRFASRIIDS LFNTVTDKKI AILGFAFKKD TGDTRESSSI YISKYLMDEG AHLHIYDPKV PREQIVVDLS HPGVSEDDQV SRLVTISKDP YEACDGAHAV VICTEWDMFK ELDYERIHKK MLKPAFIFDG RRVLDGLHNE LQTIGFQIET IGKKVSSKRI PYAPSGEIPK FSLQDPPNKK PKV.
Product Science Overview
Introduction
UDP-Glucose Dehydrogenase (UGDH) is an enzyme that plays a crucial role in the biosynthesis of glycosaminoglycans, such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosaminoglycans are essential components of the extracellular matrix and are involved in various biological processes, including cell signaling, migration, and development . The human recombinant form of this enzyme is produced using recombinant DNA technology, which allows for the expression of the enzyme in host cells such as Escherichia coli .
Preparation Methods
The preparation of human recombinant UDP-Glucose Dehydrogenase involves several steps:
- Gene Cloning: The gene encoding UGDH is cloned into an expression vector, which is then introduced into a host cell, typically Escherichia coli .
- Protein Expression: The host cells are cultured under conditions that induce the expression of the UGDH protein. This often involves the use of specific inducers and optimized growth conditions .
- Protein Purification: The expressed UGDH protein is purified using techniques such as affinity chromatography, which exploits the specific binding properties of the protein to isolate it from other cellular components .
- Quality Control: The purified protein is subjected to various quality control measures, including SDS-PAGE and activity assays, to ensure its purity and functionality .
Chemical Reactions Analysis
UDP-Glucose Dehydrogenase catalyzes the oxidation of UDP-glucose to UDP-glucuronic acid, a key step in the biosynthesis of glycosaminoglycans . The reaction involves the transfer of electrons from UDP-glucose to NAD+, resulting in the formation of UDP-glucuronic acid and NADH . The overall reaction can be summarized as follows:
This reaction is crucial for the production of glycosaminoglycans, which are important for various cellular functions and structural integrity .
Quick Inquiry
Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
