Recombinant Human All-trans-retinol dehydrogenase [NAD (ADH4) Protein (GST)

Name: Recombinant Human All-trans-retinol dehydrogenase [NAD (ADH4) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03957P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human All-trans-retinol dehydrogenase [NAD (ADH4) 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	P08319
Target Symbol	ADH4
Synonyms	Ac1002; ADH 4; ADH-1; ADH-2; ADH2; Adh4; ADH4_HUMAN; Alcohol dehydrogenase 4 (class II) pi polypeptide; Alcohol dehydrogenase 4; Alcohol dehydrogenase class II pi chain; Alcohol dehydrogenase pi isozyme ADH class II; Aldehyde reductase; Class II alcohol dehydrogenase 4 pi subunit
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGVAAGSKGLTIFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDKISEAFDLMNQGKSVRTILIF
Expression Range	1-380aa
Protein Length	Full Length
Mol. Weight	67.2kDa
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

Target Function	Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Also catalyzes the reduction of benzoquinones.
Subcellular Location	Cytoplasm.
Protein Families	Zinc-containing alcohol dehydrogenase family, Class-II subfamily
Database References	HGNC: 252 OMIM: 103740 KEGG: hsa:127 STRING: 9606.ENSP00000265512 UniGene: Hs.1219

Gene Functions References

Association between HCRTR2, ADH4,CLOCK gene polymorphisms and cluster headache was not significant in the present study. PMID: 29318394
this current study provides substantial evidence that genetic polymorphisms of rs3805322 in the ADH4 gene may be associated with an increased risk of developing ESCC in two Chinese Han populations. PMID: 26039424
This study confirmed the genetic heterogeneity of cluster headache, suggesting that mutations in the ADH4 gene might be related to cluster headache in a subset of cases. PMID: 24469609
The serum expression of ADH4 protein correlates with the progression of esophageal cancer. PMID: 24051444
expression levels of ADH4 mRNA and protein have found to be markedly reduced in hepatocellular carcinoma (HCC) tissues and significantly associated with survival. PMID: 22147505
data suggest that ADH4 intronic variants play a role in alcohol dependence susceptibility in Italian populations PMID: 22044940
Our results suggest that the analysed polymorphisms ofANKK1 and ADH4 can play an important part in the pathogenesis of alcohol abuse PMID: 22232963
the high catalytic activity of human alcohol dehydrogenase 4 studied with horse liver ADH1E PMID: 21184752
This study confirms the significant relationship of ADH4 variants with AD and related phenotypes. PMID: 20626721
Data indicate that further studies of EPHX1 rs1051740, ADH4 r1042364, and NQO1 rs291766 are needed to make more definitive conclusion on the role of variation in xenobiotic metabolism in ovarian cancer. PMID: 21480392
Our data suggest that cluster headache is associated with the ADH4 gene or a linked locus. Additional studies are warranted to elucidate the role of this gene in the etiopathogenesis of the disease. PMID: 19925625
In this study we have identified a distal upstream enhancer, 4E, of ADH4. In HepG2 human hepatoma cells, 4E increased the activity of an ADH4 basal promoter by 50-fold. 4E was cell-specific. PMID: 20363298
ADH4 gene polymorphisms are associated with upper aerodigestive tract cancers. PMID: 19861527
Thirteen new single nucleotide polymorphisms PMID: 11916005
Identification and characterisation of two allelic forms of human alcohol dehydrogenase 2 PMID: 11964133
kinetic mechanisms for ADH4 functioning as retinol dehydrogenase PMID: 11997393
Results describe the expression patterns of alcohol dehydrogenases I, III, and IV in adult rat, mouse and human tissues using radioactive oligonucleotide in situ hybridization. PMID: 12631290
The mean alcohol-elimination rate among ADH2*2 carriers is significantly higher than among ADH2*1 homozygotes in a male Jewish population. PMID: 14745297
the genotypes of six ADH4 markers were associated with alcohol dependence, and all seven ADH4 markers were associated with drug dependence PMID: 16220108
Seven single nucleotide polymorphisms spanning the ADH4 gene were genotyped in 561 subjects affected with alcohol dependence and/or drug dependence. PMID: 16237392
that personality traits and substance dependence have a partially overlapping genetic basis. PMID: 17069770
Class II alcohol dehydogenase (ADH4) is considered to contribute to ethanol oxidation in the liver at high concentration. PMID: 19182438

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.