Recombinant Human Alcohol dehydrogenase class-3 (ADH5)

Code CSB-BP001357HU
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Source Baculovirus
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Code CSB-EP001357HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-MP001357HU
Size Pls inquire
Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ADH5
Uniprot No.
Research Area
Metabolism
Alternative Names
ADH 3; ADH5; ADHX ; ADHX_HUMAN; Alcohol dehydrogenase (class III) chi polypeptide; alcohol dehydrogenase 5 (class III) chi polypeptide; Alcohol dehydrogenase 5; Alcohol dehydrogenase class 3; Alcohol dehydrogenase class chi chain; Alcohol dehydrogenase class III ; Alcohol dehydrogenase class-3; Alcohol dehydrogenase class-III; class III alcohol dehydrogenase 5 chi subunit ; FALDH; FDH; formaldehyde dehydrogenase; Glutathione dependent formaldehyde dehydrogenase; Glutathione-dependent formaldehyde dehydrogenase; GSH-FDH; GSNOR; hydroxymethyllutathione dehydrogenase; S-(hydroxymethyl)glutathione dehydrogenase
Species
Homo sapiens (Human)
Expression Region
2-374aa
Target Protein Sequence
ANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI
Mol. Weight
41.6kD
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. 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. Class-III ADH is remarkably ineffective in oxidizing ethanol.
Gene References into Functions
  1. Data (including data from studies using knockout and transgenic mice) suggest that obesity and diabetes are accompanied by decreases in GSNOR activity in hepatocytes engendering nitrosative stress; obesity promotes S-nitrosylation of lysosomal proteins in liver, thereby impairing lysosomal enzyme activities and compromising autophagy. PMID: 29074597
  2. GSNOR represents the prototype enzyme to disclose how denitrosylation plays a crucial role in tuning NO-bioactivity and how much it deeply impacts on cell homeostasis and human pathophysiology. (Review) PMID: 28533171
  3. It was concluded that in HepG2 cells, ADH5 is a source of formate for de novo purine biosynthesis, especially during folate deficiency when folate-dependent formate production is limited. PMID: 28228507
  4. GSNOR expression has different effect on neuronal viability in dependence on the stimulus applied, and plays opposite roles in SH-SY5Y models of Parkinson's disease and amyotrophic lateral sclerosis PMID: 26491229
  5. ADH5 counteracts neuronal differentiation of neural stem cells and this effect can be reversed by pharmacological inhibition of ADH5. PMID: 24895131
  6. study compared individuals occupationally exposed to formaldehyde and controls to effects of XRCC3 Thr241Met, ADH5 Val309Ile and Asp353Glu polymorphisms; ADH5 polymorphisms did not show significant association with genotoxicity biomarkers PMID: 23355119
  7. N6022 binds in the GSNO binding pocket like a competitive inhibitor, although in kinetic assays it behaves with a mixed uncompetitive mode of inhibition (MOI) toward GSNO and a mixed competitive MOI toward formaldehyde adduct S-hydroxymethylglutathione. PMID: 22335564
  8. biological significance of SNPs rs11568816, rs17028487 and rs13832 PMID: 21920416
  9. Data suggest that GSNOR deficiency, through dysregulated S-nitrosylation, may promote hepatocellular carcinoma, possibly by inactivating a DNA repair system. PMID: 20371487
  10. Significant associations were found however, for reactions to alcohol with a SNP in ADH5 (rs6827292, p = .001) and a SNP just upstream of ADH5 (rs6819724, p = .0007) that is in strong LD with rs6827292. PMID: 20158305
  11. POZ domain of FBI1 represses transcription of ADH5. PMID: 12004059
  12. The structural determination of apo, binary alcohol, and inhibitory ternary FDH complexes provides new insight into the enzyme's metal-assisted catalysis and substrate-binding properties. PMID: 12196016
  13. Formation of a FDH-S-(hydroxymethyl)glutathione-NADH ternary complex causes movement of glutathione-dependent formaldehyde dehydrogenase catalytic domain toward the coenzyme-binding domain, and a change in active-site zinc coordination. PMID: 12484756
  14. No evidence that alcohol dehydrogenase 3genotype modifies risk related to alcohol and lung cancer. PMID: 14608084
  15. data suggest that genetic variation in S-nitrosoglutathione reductase (GSNOR) might play a role in asthma susceptibility PMID: 17543375
  16. A statistically significant increase of class III alcohol dehydrogenase isoenzymes was found in the sera of pancreatic cancer patients. PMID: 18095160
  17. GSNOR inhibitors to be novel tools for regulating nitric oxide bioactivity and assessing the role of SNOs in vivo. PMID: 19596685

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Subcellular Location
Cytoplasm.
Protein Families
Zinc-containing alcohol dehydrogenase family, Class-III subfamily
Database Links

HGNC: 253

OMIM: 103710

KEGG: hsa:128

STRING: 9606.ENSP00000296412

UniGene: Hs.78989

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