UGDH Mouse
GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.
Greater than 90.0% as determined by SDS-PAGE.
Description
UGDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 57.2kDa. UGDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
The enzyme UGDH, a member of the UDP-glucose/GDP-mannose dehydrogenase family, is found in various tissues with a primary location in the liver. Its role is to convert UDP-glucose to UDP-glucuronate, a crucial step in the production of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosaminoglycans are integral components of the extracellular matrix and play a significant role in cellular processes like signal transduction, cell movement, and the progression of cancer, including its spread to other parts of the body (metastasis).
Recombinant UGDH Mouse, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 516 amino acids (specifically, amino acids 1 through 493), resulting in a molecular weight of 57.2 kDa. The protein includes a 23 amino acid His-tag attached to the N-terminus and is purified using specialized chromatographic techniques.
The UGDH protein solution has a concentration of 0.5mg/ml. It is prepared in a buffer consisting of 20mM MES (pH 5.0), 20% glycerol, 150mM NaCl, and 1mM EDTA.
For short-term storage (up to 2-4 weeks), keep the vial at a refrigerated temperature of 4°C. For extended storage, freeze the solution at -20°C. To ensure optimal preservation during long-term storage, adding a carrier protein like HSA or BSA (0.1%) is recommended. Avoid repeated cycles of freezing and thawing.
Analysis by SDS-PAGE indicates a purity level exceeding 90.0%.
The enzyme demonstrates a specific activity greater than 2,500 pmol/min/µg. This value represents the amount of enzyme required to convert 1.0 picomole of UDP-glucose to UDP-glucuronate per minute at a pH of 8.7 and a temperature of 37°C.
GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.
MGSSHHHHHH SSGLVPRGSH MGSMVEIKKI CCIGAGYVGG PTCSVIAHMC PEIRVTVVDV NEARINAWNS PTLPIYEPGL KEVVESCRGK NLFFSTNIDD AIREADLVFI SVNTPTKTYG MGKGRAADLK YIEACARRIV QNSNGYKIVT EKSTVPVRAA ESIRRIFDAN TKPNLNLQVL SNPEFLAEGT AIKDLKNPDR VLIGGDETPE GQKAVRALCA VYEHWVPKEK ILTTNTWSSE LSKLAANAFL AQRISSINSI SALCEATGAD VEEVATAIGM DQRIGNKFLK ASVGFGGSCF QKDVLNLVYL CEALNLPEVA RYWQQVIDMN DYQRRRFASR IIDSLFNTVT DKKIAILGFA FKKDTGDTRE SSSIYISKYL MDEGAHLHIY DPKVPREQIV VDLSHPGVSA DDQVSRLVTI SKDPYEACDG AHALVICTEW DMFKELDYER IHKKMLKPAF IFDGRRVLDG LHSELQTIGF QIETIGKKVS SKRIPYTPGE IPKFSLQDPP NKKPKV.
Product Science Overview
UDP-Glucose Dehydrogenase (UGDH) is an enzyme that plays a crucial role in the biosynthesis of glycosaminoglycans, such as hyaluronic acid, chondroitin sulfate, and heparan sulfate. These molecules are essential components of the extracellular matrix and are involved in various biological processes, including cell signaling, proliferation, and migration. UGDH catalyzes the oxidation of UDP-glucose to UDP-glucuronic acid, a key precursor in the synthesis of these glycosaminoglycans.
UGDH is a NAD±dependent enzyme that catalyzes the two-fold oxidation of UDP-glucose (UDP-Glc) to produce UDP-glucuronic acid (UDP-GlcA) while reducing NAD+ to NADH . This reaction is essential for the production of glycosaminoglycans, which are critical for maintaining the structural integrity of tissues and facilitating cell communication.
In mammals, UGDH is involved in the synthesis of hyaluronic acid, which is a major component of the extracellular matrix and plays a vital role in tissue hydration, lubrication, and cellular functions. The enzyme’s activity is regulated by various factors, including cytokines and growth factors. For instance, platelet-derived growth factor (PDGF) has been shown to enhance UGDH activity, leading to increased hyaluronic acid production .
Recombinant UGDH from mouse is widely used in research to study the enzyme’s structure, function, and regulation. The recombinant form allows for the production of large quantities of the enzyme, facilitating detailed biochemical and structural analyses. Studies using recombinant UGDH have provided insights into the enzyme’s catalytic mechanism and its role in various physiological and pathological processes.
The production of recombinant UGDH typically involves cloning the UGDH gene from mouse into an expression vector, which is then introduced into a suitable host organism, such as Escherichia coli. The host cells are cultured, and the recombinant enzyme is expressed and purified using techniques such as affinity chromatography. This process yields high-purity UGDH that can be used for various experimental applications.
UGDH catalyzes the oxidation of UDP-glucose to UDP-glucuronic acid through a two-step reaction mechanism. The enzyme first oxidizes UDP-glucose to UDP-glucuronic acid, generating NADH in the process. This reaction is essential for the biosynthesis of glycosaminoglycans, which are critical for maintaining the structural integrity of tissues and facilitating cell communication .
