Recombinant Human GALE Protein (N-6His)

Name: Recombinant Human GALE Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1305NP
Availability: InStock

BL-1305NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human UDP-Glucose 4-Epimerase is produced by our E.coli expression system and the target gene encoding Met1-Ala348 is expressed with a 6His tag at the N-terminus.
Accession	Q14376
Synonym	UDP-Glucose 4-Epimerase; Galactowaldenase; UDP-Galactose 4-Epimerase; GALE
Gene Background	The enzyme UDP-Glucose 4-Epimerase (GALE) is a homodimeric epimerase found in bacterial, plant and mammalian cells. UDP-Glucose 4-Epimerase performs the final step in the Leloir pathway of Galactose metabolism, it catalyzes two distinct but analogous reactions: the epimerization of UDP-Gglucose to UDP-Galactose and the epimerization of UDP-N-Acetylglucosamine to UDP-N-Acetylgalactosamine. The bifunctional nature of the enzyme has the important metabolic consequence that mutant cells (or individuals) are dependent not only on exogenous galactose, but also on exogenous N-acetylgalactosamine as a necessary precursor for the synthesis of glycoproteins and glycolipids.
Molecular Mass	40.44 KDa
Apmol Mass	35 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 50mM Tris-HCl, 150mM NaCl, 2mM DTT, 1mM EDTA, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

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 Families	NAD(P)-dependent epimerase/dehydratase family
Database References	HGNC: 4116 OMIM: 230350 KEGG: hsa:2582 STRING: 9606.ENSP00000363621 UniGene: Hs.632380
Associated Diseases	Epimerase-deficiency galactosemia (EDG)

Gene Functions References

Mutation in UDP-galactose-4'-epimerase gene is associated with UDP-galactose-4'-epimerase deficiency. PMID: 26565537
Data show the protein structure of GALE and its substrate binding and specificity. It is mutated in type III galactosemia. [review] PMID: 26162744
human UDP-galactose 4'-epimerase stability is increased by variants associated with type III galactosemia but decreased by substrate and cofactor binding PMID: 25150110
These data indicated a critical role of GALE in maintaining cartilage homeostasis, and suggested that GALE inhibition might contribute to OA progress. PMID: 25201731
GALE variants can be arranged into three groups depending on the severity of enzyme impairment. PMID: 23644136
P.K161N-hGALE causes its effects by abolishing an important interaction between the protein and the cofactor. PMID: 22613355
study of hGALE crystal structure and demonstration that residue 307 acts as a gatekeeper mediating substrate access to the hGALE active site PMID: 15175331
Resulst describe the relationship among UDP-galactose 4'-epimerase activity, substrate specificity, metabolic balance, and galactose sensitivity in mammalian cells. PMID: 15701638
Data suggest that reduced catalytic efficiency and increased proteolytic susceptibility of UDP-galactose 4-epimerase are causative factors in type III galactosemia. PMID: 16302980
Subtle biochemical and metabolic abnormalities detected in patients expressing these GALE alleles likely reflect, at least in part, the reduced enzymatic activity of the encoded GALE proteins. PMID: 18188677
Our observations show that altered protein stability is due to misfolding and that loss or reduction of enzyme activity is responsible for the molecular defects underlying GALE-deficiency galactosemia. PMID: 19250319
Disease-causing mutations result in a variety of changes to the steady-state parameters. Mostly these are changes in turnover number, kcat. The ability to dimerize is not affected, but some mutants have increased sensitivity to protease digestion. PMID: 16302980

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.