Human GALE (Udp-Glucose 4-Epimerase) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-04669P
SDS-PAGE analysis of Human GALE (Udp-Glucose 4-Epimerase) - Recombinant Protein, CAT
SDS-PAGE analysis of Human GALE (Udp-Glucose 4-Epimerase) - Recombinant Protein, CAT# BLT-04669P, showing >90% purity under 15% SDS-PAGE (Reduced)

Human GALE (Udp-Glucose 4-Epimerase) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-04669P
Regular price $595.00 Sale price $475.00Save $120
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500 µg $1,100 (Summer Promotion)
1 mg $1,990 (Summer Promotion)

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Product Overview

Product Name Recombinant Human UDP-Glucose 4-Epimerase/GALE Protein
Product Overview This recombinant human UDP-Glucose 4-Epimerase/GALE protein includes amino acids 1-348aa of the MAPT gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id Q14376
Recommended Name UDP-glucose 4-epimerase
Gene Name GALE
Synonyms UDP-Glucose 4-Epimerase; Galactowaldenase; UDP-Galactose 4-Epimerase; GALE
Species Human
Predicted Molecular Mass 40.4 kDa
Expression System E.coli
Expression Range 1-348aa
Tag N-6His
Purity >90%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Cell Biology
Target Function Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6-phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids.
Protein Family NAD(P)-dependent epimerase/dehydratase family
Associated Diseases Epimerase-deficiency galactosemia (EDG)

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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