Recombinant Mouse ASAH2 Protein (His Tag)(Active) | PKSM040922

Recombinant Mouse ASAH2 Protein (His Tag)(Active) | PKSM040922 | Gentaur US, UK & Europe Disrtribition

Synonyms: AI585898

Active Protein: Active protein

Activity: A DNA sequence encoding the Lumenal domain (Thr 34-Thr 756) of mouse ASAH2 (NP_061300.1) precursor was expressed with a N-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the Lumenal domain (Thr 34-Thr 756) of mouse ASAH2 (NP_061300.1) precursor was expressed with a N-terminal polyhistidine tag.

Fusion Tag: N-His

Species: Mouse

Expressed Host: HEK293 Cells

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

Purity: > 97 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

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: 82 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

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

Background: ASAH2 (N-acylsphingosine amidohydrolase 2), also known as neutral ceramidase, is a type II integral membrane protein that can be cleaved to produce a soluble secreted protein. The enzyme is abundant in the brush border membranes of the intestine, and also expressed in several tissues such as kidney, brain and liver. The primary structure of ASAH2/neutral ceramidase is highly conserved from bacteria to humans, however, there is a clear difference in the molecular architecture. The murine ASAH2 possesses ‘amucin box’, a Ser/Thr/Pro-rich domain glycosylated with O-glycans which is necessary to retain the enzyme on the plasma membrane as a type II integral protein. The major physiological function of ASAH2/neutral ceramidase is the metabolism of dietary sphingolipids, and thus plays a role in the generation of messenger molecules such as sphingosine and sphingosine 1-phosphate.

Research Area: N/A