Alcohol Dehydrogenase 5 (Class III), chi Polypeptide (ADH5) ELISA Kits

ADH5 encodes class V alcohol dehydrogenase, which is a member of the alcohol dehydrogenase family. Zusätzlich bieten wir Ihnen Alcohol Dehydrogenase 5 (Class III), chi Polypeptide Antikörper (119) und Alcohol Dehydrogenase 5 (Class III), chi Polypeptide Proteine (31) und viele weitere Produktgruppen zu diesem Protein an.

list all ELISA KIts Gen GeneID UniProt
ADH5 128 P11766
Anti-Ratte ADH5 ADH5 100145871 P12711
ADH5 11532 P28474
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Katalog Nr. Reaktivität Sensitivität Bereich Bilder Menge Anbieter Lieferzeit Preis Details
Human 6.7 pg/mL 15.625 pg/mL - 1000 pg/mL Typical Standard Curve 96 Tests Anmelden zum Anzeigen 15 bis 17 Tage
$908.41
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  96 Tests Anmelden zum Anzeigen 16 bis 21 Tage
$1,161.29
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Weitere ELISA Kits für Alcohol Dehydrogenase 5 (Class III), chi Polypeptide Interaktionspartner

Human Alcohol Dehydrogenase 5 (Class III), chi Polypeptide (ADH5) Interaktionspartner

  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.

  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)

  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.

  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

  5. ADH5 counteracts neuronal differentiation of neural stem cells and this effect can be reversed by pharmacological inhibition of ADH5.

  6. common ADH variants conferred risk for both schizophrenia in African-Americans and autism in European-Americans.

  7. A decrease in ADH IB, rather than GSNOR, correlates with human lung cancer.

  8. 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

  9. 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.

  10. biological significance of SNPs rs11568816, rs17028487 and rs13832

  11. Data suggest that GSNOR deficiency, through dysregulated S-nitrosylation, may promote hepatocellular carcinoma, possibly by inactivating a DNA repair system.

  12. 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.

  13. POZ domain of FBI1 represses transcription of ADH5.

  14. 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.

  15. 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.

  16. No evidence that alcohol dehydrogenase 3genotype modifies risk related to alcohol and lung cancer.

  17. data suggest that genetic variation in S-nitrosoglutathione reductase (GSNOR) might play a role in asthma susceptibility

  18. A statistically significant increase of class III alcohol dehydrogenase isoenzymes was found in the sera of pancreatic cancer patients.

  19. GSNOR inhibitors to be novel tools for regulating nitric oxide bioactivity and assessing the role of SNOs in vivo.

  20. Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.

Mouse (Murine) Alcohol Dehydrogenase 5 (Class III), chi Polypeptide (ADH5) Interaktionspartner

  1. Site-directed mutagenesis of Akt at Cys224 revealed that S-nitrosylation at this site was pivotal for the reduced phosphorylation at Akt Ser473, which led to impaired Akt signaling. Furthermore, on HHcy challenge, as compared with GSNOR(+/+)ApoE(-/-) littermate controls, GSNOR(-/-)ApoE(-/-) double knockout mice showed reduced T-cell activation with concurrent reduction of atherosclerosis.

  2. 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.

  3. Report inhibition of GSNOR activity by nebivolol leading to accumulation of nitrosothiols in cells, and this is associated with an enhanced vasodilation by S-nitrosoglutathione.

  4. Increased GSNOR expression during aging decreases S-nitrosation of CaMKIIalpha and reduces CaMKIIalpha synaptosomal accumulation.

  5. These data indicate a role for GSNOR in the host response to malaria infection and suggest that strategies to disrupt its activity will improve clinical outcomes.

  6. GSNOR may act as a "brake" on skeletal muscle contractile performance under physiological conditions by modulating nitrosylation/denitrosylation balance.

  7. Loss of GSNOR confers enhanced post-MI cardiac regenerative activity, characterized by enhanced turnover of cardiomyocytes and cardiac stem cells.

  8. Results show that ADH5 removes endogenous formaldehyde to prevent DNA adducts, and protects with FANCD2, hematopoietic stem cells, hepatocytes, and nephrons from endogenous DNA damage.

  9. S-nitrosoglutathione reductase-dependent modification of PPARgamma alters the balance between adipocyte and osteoblast differentiation and provides checkpoint regulation of the lineage bifurcation of these 2 lineages.

  10. These findings provide novel insights into the involvement of GSNOR and S-nitrosylation in neuromuscular atrophy and neuropathic pain that are associated with pathological states.

  11. Overexpression of ADH5 reduces both development and adult neuronal differentiation of neurons. This effect depends on the catalytic activity of ADH5 and involves ADH5-mediated denitrosation of histone deacetylase 2 (HDAC2).

  12. GSNOR appears to play a crucial role in controlling pulmonary and systemic infection by K. pneumoniae.

  13. A critical role for GSNOR in maintaining genomic integrity.

  14. This study suggests that S-nitrosoglutathione reductase degradation of S-nitrosoglutathione is a vital step in the expression of ventilatory roll-off

  15. GSNOR deficiency has a role in hepatocarcinogenesis, which is prevented by iNOS inhibition

  16. Increasing the denitrosylation capacity of cardiomyocytes, via cardiomyocyte-specific overexpression of GSNOR, protects against sepsis-induced myocardial depression.

  17. Compared the protein expression profiles in the livers of wild-type and GSNOR-deficient (GSNOR(-/-) ) mice that were challenged with lipopolysaccharide; subsequently id'd 19 upregulated and 19 downregulated proteins in GSNOR(-/-) mice using mass spec.

  18. These results indicate that systemic hemodynamic responses (vascular tone and cardiac contractility), both under basal conditions and after adrenergic activation, are regulated through concerted actions of NO synthase/GSNOR.

  19. protection of AGT and resistance to nitrosamine-induced genotoxicity critically depends on GSNOR in hepatocytes

  20. Data show that GSNO-R activity was elevated in lung homogenates from female compared to male mice.

Alcohol Dehydrogenase 5 (Class III), chi Polypeptide (ADH5) Antigen-Profil

Beschreibung des Gens

This gene encodes a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis. The human genome contains several non-transcribed pseudogenes related to this gene.

Genbezeichner und Symbole assoziert mit ADH5

  • alcohol dehydrogenase 5 (class III), chi polypeptide (ADH5) Antikörper
  • alcohol dehydrogenase 5 (adh5) Antikörper
  • alcohol dehydrogenase 5 (class III), chi polypeptide (Adh5) Antikörper
  • alcohol dehydrogenase 5 (class III), chi polypeptide L homeolog (adh5.L) Antikörper
  • adh-3 Antikörper
  • Adh-5 Antikörper
  • ADH1C Antikörper
  • adh3 Antikörper
  • ADH4 Antikörper
  • adh5 Antikörper
  • adhx Antikörper
  • FALDH Antikörper
  • fdh Antikörper
  • GSH-FDH Antikörper
  • gsnor Antikörper
  • wu:fb60b11 Antikörper

Bezeichner auf Proteinebene für ADH5

S-(hydroxymethyl)glutathione dehydrogenase , alcohol dehydrogenase (class III), chi polypeptide , alcohol dehydrogenase class chi chain , alcohol dehydrogenase class-3 , alcohol dehydrogenase class-III , formaldehyde dehydrogenase , glutathione-dependent formaldehyde dehydrogenase , FALDH , FDH , GSH-FDH , alcohol dehydrogenase 1C (class I), gamma polypeptide , class III alcohol dehydrogenase , fb60b11 , ADH-B2 , alcohol dehydrogenase 2 , alcohol dehydrogenase B2 , class III alcohol dehydrogenase, chi subunit , S-nitrosoglutathione reductase , alcohol dehydrogenase 5 (class III), chi polypeptide L homeolog , alcohol dehydrogenase class 3 , alcohol dehydrogenase 4 (class II), pi polypeptide

GENE ID SPEZIES
128 Homo sapiens
100009307 Oryctolagus cuniculus
116517 Danio rerio
100145871 Rattus norvegicus
11532 Mus musculus
505515 Bos taurus
100719427 Cavia porcellus
445841 Xenopus laevis
609781 Canis lupus familiaris
422705 Gallus gallus
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