Recombinant Human AKR1A1 Protein (His Tag) | PKSH031070

Recombinant Human AKR1A1 Protein (His Tag) | PKSH031070 | Gentaur US, UK & Europe Disrtribition

Synonyms: ALDR1;ALR;ARM;DD3;HEL-S-6

Active Protein: N/A

Activity: A DNA sequence encoding the human AKR1A1 (P14550) (Met 1-Tyr 325) was expressed, with a polyhistidine tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human AKR1A1 (P14550) (Met 1-Tyr 325) was expressed, with a polyhistidine tag at the N-terminus.

Fusion Tag: N-His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 39 kDa

Formulation: Lyophilized from sterile PBS, pH 7.5

Reconstitution: Please refer to the printed manual for detailed information.

Background: Aldehyde reductase (AKR1A1) is a member of the aldo-keto reductase superfamily, which consists of more than 40 known enzymes and proteins that includes variety of monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase. Aldehyde reductase has wide substrate specificities for carbonyl compounds. These enzymes are implicated in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. Aldehyde reductase possess a structure with a beta-alpha-beta fold which contains a novel NADP-binding motif. The binding site is located in a large, deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases. AKR1A1 is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue.

Research Area: Signal Transduction, Cell biology, Cancer, metabolism,