Human Alcohol Dehydrogenase 2 (ADH2) Protein

Este producto es parte de ADH - Alcohol dehydrogenase
Human Alcohol Dehydrogenase 2 (ADH2) Protein
208€ (10 µg)

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Name
Human Alcohol Dehydrogenase 2 (ADH2) Protein
Category
Proteins and Peptides
Provider
Abbexa
Reference
abx652443
Tested Applications
WB, SDS-PAGE

Description

Human Alcohol Dehydrogenase 2 (ADH2) Protein is a recombinant Human protein expressed in E. coli.

Documentos del producto

Instrucciones
Data sheet
Descargar

Especificaciones del producto

Category
Proteins and Peptides
Immunogen Target
Alcohol Dehydrogenase 2 (ADH2)
Host
E. coli
Assay Type
Activity: Not tested
Sequence Fragment: Ser2-Phe375
Tag: N-terminal His tag
Origin
Human
Conjugation
Unconjugated
Expression
Recombinant
Purity
> 90%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 5-7 working days.
Storage
Store lyophilized form at 2-8°C for up to 1 month. For longer periods, store lyophilized or liquid at -80°C. Avoid repeated freeze–thaw cycles.
Dry Ice
No
Alias
ADH1B,ADH2, HEL-S-117
Background
Protein ADH1B
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.
To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Concentration: Prior to lyophilization: 200 µg/ml

Background

ADH1B encodes the beta subunit of class I ADH enzymes, which are highly active in the oxidation of ethanol to acetaldehyde. This subunit is particularly important in liver and stomach tissues, where alcohol metabolism is initiated. Polymorphisms in the ADH1B gene, such as the ADH1B2 and ADH1B3 variants, are known to significantly alter enzyme activity. These variants exhibit faster ethanol oxidation rates and are associated with reduced risks of alcohol dependence and increased susceptibility to alcohol-induced flushing. ADH1B also participates in the metabolism of other alcohols and aldehydes, influencing various physiological and pathological processes. Its role in retinol metabolism connects it to pathways involved in vision and cell differentiation. Dysregulation of ADH1B activity has implications for alcohol-related liver diseases and certain cancers, particularly those of the gastrointestinal tract, where acetaldehyde accumulation is a risk factor.

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