Recombinant Human Galactose-1-Phosphate Uridylyltransferase (GALT) Protein (His-SUMO)

Name: Recombinant Human Galactose-1-Phosphate Uridylyltransferase (GALT) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04326P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Galactose-1-Phosphate Uridylyltransferase (GALT) 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	P07902
Target Symbol	GALT
Synonyms	Gal 1 P uridylyltransferase; Gal-1-P uridylyltransferase; Galactose 1 phosphate uridyl transferase; Galactose 1 phosphate uridylyltransferase; Galactose-1-phosphate uridylyltransferase; GALT; GALT_HUMAN; UDP glucose hexose 1 phosphate uridylyltransferase; UDP-glucose--hexose-1-phosphate uridylyltransferase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHLGQKDRETATIA
Expression Range	1-379aa
Protein Length	Full Length
Mol. Weight	59.4kDa
Research Area	Metabolism
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	Plays an important role in galactose metabolism.
Protein Families	Galactose-1-phosphate uridylyltransferase type 1 family
Database References	HGNC: 4135 OMIM: 230400 KEGG: hsa:2592 STRING: 9606.ENSP00000368119 UniGene: Hs.522090
Associated Diseases	Galactosemia (GALCT)

Gene Functions References

GALT mutation is associated with galactosemia. PMID: 29252199
The mutational spectrum of the GALT gene in Greek galactosemia patients is presented for the first time. PMID: 28644047
novel splicing mutation in GALT gene causing Galactosemia in Ecuadorian family PMID: 28450132
17 VUS (37%; 7 in ACADM, 9 in GALT, and 1 in PAH) were reclassified from uncertain (6 to benign or likely benign and 11 to pathogenic or likely pathogenic). We identified common types of missing information that would have helped make a definitive classification and categorized this information by ease and cost to obtain PMID: 27308838
we present the 1.9 A resolution crystal structure of human GALT (hGALT) ternary complex, revealing a homodimer arrangement that contains a covalent uridylylated intermediate and glucose-1-phosphate in the active site, as well as a structural zinc-binding site, per monomer PMID: 27005423
A novel noncoding homozygous GALT variant associated with asymptomatic galactosemia has been described in an infant of consanguineous heterozygous parents. PMID: 25920691
Mutation activates a cryptic donor splice site, inducing an aberrant splicing of the GALT pre-mRNA, which in turn leads to a frameshift with inclusion of a premature stop codon. PMID: 25052314
GALT activity in red blood cells of patients with galactosaemia PMID: 25268296
Novel missense mutations identified in Italian galactosemic patients. PMID: 25592817
In Korean population, novel GALT mutations were identified in the galactosemia patients different from those of other populations. PMID: 25124065
suggests that GALT mutations are ethnic-specific and that galactosemia is a heterogeneous disorder at the molecular level PMID: 24045215
In this report, we present GALT gene mutations in 56 cases of galactosemia from Turkey identified using DNA microarray resequencing. PMID: 23924834
Data suggest that in classic galactosemia residual GALT activity (predicted from activity of recombinant GALT matching patient's mutation) correlates with reduced ovarian reserve (as indicted by biological marker, circulating anti-Mullerian hormone). PMID: 23690308
HGALT requires a level of flexibility to function optimally and that altered folding is the underlying reason of impairment in all the variants tested here. PMID: 23583749
The study determined the frequency of the two most common GALT mutations and their variants in Indian galactosemia patients. PMID: 22798028
The novel GALT gene mutations included 6 missense mutations viz. Y89H, Q103R, P166A, S181F, K285R, R333L; one nonsense mutation, S307X and 3 silent mutations--Q103Q, K210K and H319H. PMID: 23022339
Forty four novel variations in the GALT gene were identified, among them 27 nucleotide substitutions, in the French cohort of galactosemic patients. PMID: 22944367
Mutations of the galactose-1-phosphate uridyltranseferase gene is associated with galactosemia. PMID: 22963887
Duarte1 (D1) and D2 genotypes of GALT do not appear to play a role in the association between galactose intake, possible ovarian dysfunction, and the link with ovarian cancer PMID: 22749219
3 different GALT mutations viz. Q188R, N314D and S307X were found to be present in the family of a neonate diagnosed with galactosemia and having the heterozygote genotype Q188R/S307X. S307X is a novel GALT mutation linked to galactosemia. PMID: 21188552
Results suggest that classical galactosaemia shows low allelic heterogeneity in Mexican patients. PMID: 18956253
Congenital eye abnormalities and galactosemia were found in a family with Q188R and G1391A mutations. PMID: 20222886
GALT deletion mutation carrier frequency was 1 in 127 (0.79%). PMID: 21059483
live birth incidence of classical galactosemia in Estonia is 1:19.700 PMID: 20151200
The simulated point mutations have a direct effect on the active site, or on the dimer assembly and stability, or on the monomer stability. PMID: 20008339
no effect seen of N314D GALT genotype on risk of borderline or invasive ovarian cancer PMID: 11936817
Data found no association between congenital absence of the uterus and vagina (CAUV) and the N314D allele of the galactose-1-phosphate uridyl transferase (GALT) gene. PMID: 12606594
Increased expression of Galactosyltransferase is associated with ovarian cancer PMID: 12851678
association of decreased galactose-1-phosphate uridyltransferase activity with idiopathic presenile cataract PMID: 14707519
children and adolescents with galactosemia function generally within the low average IQ range and have less well-developed executive functions. PMID: 15506833
No statistically significant differences were observed in the allele frequencies between the infertile women and control groups for GALT PMID: 15749517
Nine novel mutations in the GALT gene associated with Classical galctosemia are described. PMID: 15841485
No association of GALT mutations is found in 86 patients with idiopathic premature ovarian failure. PMID: 16009197
We postulate that molecular link between defective GALT enzyme, which result in classic galactosemia and the cerebroside galactosyl transferase, responsible for galactosylation of cerebrosides, is dependent on concentrations of UDP-galactose. PMID: 16125333
no relationship was found between ovarian failure and GALT polymorphisms in Indian women PMID: 16274605
no significant differences between women carrying at least one N314D or Q188R GALT allele and controls in IVF outcomes measured: numbers of follicles and oocytes obtained; fertilization rates and percentage of Grade A embryos; and pregnancy rates. PMID: 16595241
analysis of classical galactosaemia mutations in GALT1 in Spain and Portugal PMID: 17041746
analysis of a patient with galactose-1-phosphate uridyltransferase mutations p.Q188R and p.R333W and galactose metabolite levels during breast-feeding [case report] PMID: 17143577
Identified novel mutations in GALT gene using DNA testing. PMID: 17876724
The R204X mutation severely compromises both expression and function of human GALT;T268N is one of a very small number of naturally occurring rare but neutral missense polymorphisms in human GALT. PMID: 18210213
Synergistic effect of GALT and lactase mutations on cataract formation. PMID: 18454942
4 bp 5' deletion in GALT is a causal mutation in Duarte galactosemia. PMID: 19224951
Galactose-1-phosphate uridyl transferase deficiency is not associated with Mullerian aplasia in Dutch patients PMID: 19646668

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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.