Recombinant Human Alcohol Dehydrogenase 1C (ADH1C) Protein (GST)

Name: Recombinant Human Alcohol Dehydrogenase 1C (ADH1C) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09191P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Alcohol Dehydrogenase 1C (ADH1C) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00326
Target Symbol	ADH1C
Synonyms	ADH gamma subunit; ADH1C; ADH1G_HUMAN; Adh3; Alcohol dehydrogenase 1C (class I) gamma polypeptide; Alcohol dehydrogenase 1C; Alcohol dehydrogenase 1C gamma polypeptide; Alcohol dehydrogenase 3 (class I) gamma polypeptide; Alcohol dehydrogenase 3; Alcohol dehydrogenase subunit gamma; Aldehyde reductase; Class I alcohol dehydrogenase; OTTHUMP00000220209
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNPRGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGFDLLRSGKSIRTVLTF
Expression Range	1-375aa
Protein Length	Full Length
Mol. Weight	66.7kDa
Research Area	Signal Transduction
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.
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

Subcellular Location	Cytoplasm.
Protein Families	Zinc-containing alcohol dehydrogenase family
Database References	HGNC: 251 OMIM: 103730 KEGG: hsa:126 UniGene: PMID: 28239076 Expression of xylanase under the regulation of ADH3, AOX1 and GAP was compared.The highest enzyme production was obtained with AOX1 culture at shake-flask level.The PADH3 cultures were more productive than AOX1 and GAP at fermentor scale PMID: 26835836 The ADH1C 1/2 polymorphism is likely associated with pancreatitis risk. PMID: 26634490 the combination of genotypes ADH2 * 2, CYP2E1 * 1 combined with genotype homozygous ALDH2 * 1 found in this study could be leading to the population to a potential risk to alcoholism. The role of ADH3 was not indicated. PMID: 26848198 Thus these findings suggest that the three variants of ADH1C, MnSOD and GSTM1 can be used to identify individuals who are at high risk to develop ALD and may be helpful in proper management of Indian alcoholics PMID: 26937962 Results show that mutation of this protein confers associated protection against alcohol dependence. However these associations were not completely independent PMID: 24735490 Among the Inuit in Greenland, ADH1C SNPs play a role in shaping their alcohol drinking patterns. PMID: 25311581 findings suggest that ADH1C2 is associated with alcohol dependence in the Turkish population displaying a dominant inheritance model. ADH1C2 allele may contribute to the variance in heritability of alcohol dependence. PMID: 25372623 Young male East Indians with at least one ADH1C2 allele feel less effects of alcohol, including nausea. PMID: 25208201 a positive association between inactive ADH1C G allele and alcohol consumption regarding gastric cancer risk was found, opposite to that found in previous studies PMID: 25524923 Decreased expression of ADH1C gene is associated with disease progression. PMID: 24599561 Alcohol dehydrogenase (ADH)1B and ADH1C are jointly associated with alcohol use disorders, but not consumption. PMID: 23895337 additional support for the association of SNP rs1614972 in ADH1C with alcohol dependence PMID: 23516558 ADH1C polymorphism is not associated with childhood acute leukemia and maternal caffeinated beverage consumption during pregnancy. PMID: 23404349 study failed to find any link between the ADH1C genotype and the cardioprotective effects of alcohol PMID: 23321361 did not observe association of ADH1C polymorphism with esophageal cancer PMID: 22930414 The frequency of ALDH22 and ADH31 alleles in risk drinkers was lower than that in safe drinkers in a male Tibetan population. PMID: 22279680 No associations between alcohol dependence and polymorphisms in ADH1C were found in Mexican and Native Americans PMID: 22931071 Findings suggest that a significantly higher presence of ADH1C2 allele is associated with alcohol dependence in a Turkish population. PMID: 22414625 This meta-analysis suggests that ADH1C polymorphism may not be associated with breast cancer development in Caucasians. PMID: 22353233 ADH1C Ile350Val polymorphism may contribute to cancer risk among Africans and Asians. PMID: 22675424 findings support that ADH1C Ile may lower the risk of alcohol dependence and alcohol abuse as well as alcohol-related cirrhosis in pooled populations, with the strongest and most consistent effects in Asians PMID: 22476623 in a study of alcohol metabolic genotypes in drunk drivers, the rs698 ADH1C and rs671 ALDH2 polymorphisms were not associated with MCV PMID: 21917409 No profound connection between alcohol dependence and ADH1C Ile350Val gene polymorphism was detected. PMID: 22325912 This study shows differences in the distribution of the frequency of allele ADH1C1 between the Basque Country and Moroccan populations, and a new allele not described to date. PMID: 21303386 This study suggested that the ADH1C Sspl polymorphism could play a significant role in the etiology of oral cancer. PMID: 21705789 The presence of ADH3 in normal lung development (A549 cell line), & the capacity to convert retinol to retinoic acid, indicates that fetal human lung has the ability to regulate the supply of vitamin A from the pseudoglandular stage. PMID: 21482329 the ADH1C2/2 genotype was associated with a 42% increase in risk of colorectal cancer when compared with the ADH1C1/1 genotype. PMID: 21163612 Polymorphisms in ADH1C is associated with pancreatic cancer. PMID: 19068087 The increased risk of oral clefts was evident only in mothers or children who carried the ADH1C haplotype associated with reduced alcohol metabolism. PMID: 20810466 These findings suggest that a lower presence of ADH1C1 allele is associated with squamous cell carcinoma of the head and neck PMID: 20448861 Among variant allele carriers of ADH1C Arg(272)Gln, alcohol intake increased the risk of breast cancer with 14% (95% CI: 1.04-1.24) per 10g alcohol/day. PMID: 20350778 Results suggest that the ADH1C allele modifies the carcinogenic dose response for alcohol in the upper aerodigestive tract, giving rise to a gene-environment interaction. PMID: 20437850 ADH1C polymorphisms were not significantly associated with pancreatic cancer risk. PMID: 19812523 Besides the identification of new genetic factors related to alcohol biodisposition relevant to whites, this study provides unambiguous identification of diplotypes related to variability in alcohol biodisposition. PMID: 20101753 ADH1C gene polymorphisms are associated with upper aerodigestive tract cancers. PMID: 19861527 Report associations between genetic variation of alcohol dehydrogenase type 1C (ADH1C), alcohol consumption, and metabolic cardiovascular risk factors. PMID: 19447389 A new coding variant has been identified at codon 351 of ADH1C, an allele found in most Native American populations studied, with allele frequencies of the new ADH1C*351Thr allele as high as 26%. PMID: 12500098 Results suggest that alcohol dehydrogenase 3 catalysed S-nitrosoglutathione reduction is of physiological relevance in the metabolism of NO in humans. PMID: 12631283 There is no significant interaction between alcohol consumption and ADH3 genotype. PMID: 12658118 adh3 gene is implicated in alcoholism incidence among African Americans PMID: 12713190 gastric ADH3 may highly effectively contribute to the first-pass metabolism at 0.5-3 M ethanol, an attainable range in the gastric lumen during alcohol consumption PMID: 12782305 mutations in genes encoding ADH1C (G78Stop) as genetic risk factors for Parkinson disease . PMID: 15642852 ADH1C polymorphisms in the cis-acting elements affect transcription. PMID: 15643610 a slower alcohol clearance rate is associated with the ADH3 y2 allele [letter] PMID: 15842377 mean corpuscular volume values were not associated with genotype polymorphisms of ADH1C PMID: 15897724 No association has been revealed for the alcohol metabolism-related ADH3 genotype and Korean patients with alcoholism compared to Korean control subjects without alcoholism. PMID: 15902904 Conversely, in both genders, no differences were found between ADH3 genotypes regarding all cardiovascular risk factors studied and carotid intima-media thickness. PMID: 15941567 ADH1C genotype modifies the association between alcohol consumption and HDL levels among men and postmenopausal women not using postmenopausal hormones who drink moderately PMID: 16051248 Alcohol dehydrogenase 3 null genotypes did not modify the risk of HCC due to alcohol intake. PMID: 16132793

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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.

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