Recombinant Human ADSL/Adenylosuccinate Lyase Protein (His Tag) | PKSH031168

Recombinant Human ADSL/Adenylosuccinate Lyase Protein (His Tag) | PKSH031168 | Gentaur US, UK & Europe Disrtribition

Synonyms: AMPS;ASASE;ASL

Active Protein: N/A

Activity: A DNA sequence encoding the human ADSL (P30566-1) (Met 1-Leu 484) was expressed, with a polyhistidine tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human ADSL (P30566-1) (Met 1-Leu 484) 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: > 95 % 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: 57 kDa

Formulation: Lyophilized from sterile PBS, 10% glycerol, pH 7.5

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

Background: Adenylosuccinate lyase, also known as adenylosuccinase, ADSL or ASL, is an enzyme implicated in the reaction of adenylosuccinat converting to AMP and fumarate as part of the purine nucleotide cycle. The two substates of adenylosuccinate lyase (ADSL) are dephosphorylated derivatives of SAICA ribotide (SAICAR) and adenylosuccinate (S-AMP), which catalyzes an important reaction in the de novo pathway of purine biosynthesis. ADSL catalyzes two distinct reactions in the synthesis of purine nucleotides, both of which involve the _-elimination of fumarate to produce either aminoimidazole carboxamide ribotide from SAICAR or AMP from S-AMP. The Adenylosuccinate lyase deficiency is a rare autosomal recessive metabolic disorder characterized by the present of SAICA riboside and succinyladenosine (S-Ado). ADSL defect in different patients is often caused by different mutations to the enzyme.

Research Area: N/A