ADH7 Protein (AA 1-374) (His tag)

Catalog No. ABIN7557838

This Recombinant ADH7 protein is produced in HEK-293 Cells.

Quick Overview for ADH7 Protein (AA 1-374) (His tag) (ABIN7557838)

Target: ADH7 (Alcohol Dehydrogenase 7 (Class IV), mu Or sigma Polypeptide (ADH7))

Protein Type: Recombinant

Origin: Mouse

Source: HEK-293 Cells

Purity: > 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)

Grade: custom-made

Product Details

Protein Characteristics: AA 1-374

Purification tag / Conjugate: This ADH7 protein is labelled with His tag.

Purpose: Predefined custom protein recombinant Adh7 Protein expressed in mammalian cells.

Sequence: MGTAGKVIKC KAAVLWGVNQ PFSIEEIEVA PPKAKEVRVK ILATGICRTD DHIIKGSMVS KFPVIVGHEA VGVVESVGEG VTTVRPGDKV IPLFLPQCRE CNACLNPEGN LCIRSDLTGR GVLADGTTRF TCKGKPVQHF MNTSTFTEYT VLDESSVAKV DGAAPPEKAC LIGCGFSTGY GAAVKTAKVT PGSTCVVFGL GGVGLSVIMG CKAAGASRII GIDINKDKFQ KALAVGATEC ISPKDSTKPI SEVLSDMTGN TIQYTFEVIG RLETMVDALS SCHMNYGTSV VVGAPPSAKM LTYDPMLLFT GRTWKGCVFG GWKSRDDVPK LVTEFLEKKF DLDQLITHTL PFNNINEGFE LLYSGKSIRT VLTF Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If you have a special request, please contact us.

Specificity: If you are looking for a specific domain and are interested in a partial protein or a different isoform, please contact us regarding an individual offer.

Characteristics: Key Benefits:

• Predefined custom protein - from design to production - by highly experienced protein experts.
• Protein expressed in mammalian cells and purified in one-step affinity chromatography
• The optimized expression system ensures reliability for intracellular, secreted and transmembrane proteins.
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a predefined protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.

If you are not interested in a full length protein, please contact us for individual protein fragments.

The big advantage of ordering our predefined custom proteins in comparison to ordering custom-made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

Application Details

Application Notes: We expect the protein to work for functional studies. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

Target: ADH7 (Alcohol Dehydrogenase 7 (Class IV), mu Or sigma Polypeptide (ADH7))

Alternative Name: Adh7

Background: All-trans-retinol dehydrogenase [NAD(+)] ADH7 (EC 1.1.1.105) (ADH-C2) (Alcohol dehydrogenase 7) (Alcohol dehydrogenase class 4 mu/sigma chain) (EC 1.1.1.1) (Alcohol dehydrogenase class IV mu/sigma chain) (Gastric alcohol dehydrogenase) (Omega-hydroxydecanoate dehydrogenase ADH7) (EC 1.1.1.66) (Retinol dehydrogenase),FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, aldehyde and omega-hydroxy fatty acids and their derivatives. Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid. In vitro can also catalyzes the NADH-dependent reduction of all-trans-retinal and aldehydes and their derivatives. Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and hexanal. Catalyzes in the oxidative direction with higher efficiency. Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation. {ECO:0000250|UniProtKB:P40394}.

Molecular Weight: 39.9 kDa

UniProt: Q64437

AlphaFold: Q64437