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

Name: Recombinant Human Udp-Glucose 4-Epimerase (GALE) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09920P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Udp-Glucose 4-Epimerase (GALE) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14376
Target Symbol	GALE
Synonyms	FLJ95174; FLJ97302; Galactose 4 epimerase UDP; Galactowaldenase; galE; GALE_HUMAN; OTTHUMP00000002991; OTTHUMP00000002994; OTTHUMP00000037931; OTTHUMP00000044857; SDR1E1; short chain dehydrogenase/reductase family 1E member 1; UDP galactose 4 epimerase; UDP galactose 4' epimerase; UDP glucose 4 epimerase; UDP-galactose 4-epimerase; UDP-glucose 4-epimerase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA
Expression Range	1-348aa
Protein Length	Full Length
Mol. Weight	54.3kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	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%.
Storage	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.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.