Recombinant Human cathepsin A is produced by our mammalian expression system in human cells. The target protein is expressed with sequence (Ala29Tyr480) of Human cathepsin A fused with a polyhistidine tag at the C-terminus.
Reinheit
> 95 % as determined by reducing SDS-PAGE.
Sterilität
0.2 μm filtered
Endotoxin-Niveau
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
CTSA
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
> 90 % as determined by reducing SDS-PAGE.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Rekonstitution
It is not recommended to reconstitute to a concentration less than 100 μg/mL. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Buffer
Supplied as a 0.2 μm filtered solution of 20 mM PB,150 mM NaCl, pH 7.4.
Handhabung
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Lagerung
-80 °C
Informationen zur Lagerung
Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
Cathepsin A is active in cellular compartments called lysosomes. These compartments contain enzymes that digest and recycle materials when they are no longer needed. Cathepsin A interacts with the enzymes β-galactosidase and neuraminidase 1, which play a role in the breakdown of complexes of sugar molecules (oligosaccharides) attached to certain proteins (glycoproteins) or fats (glycolipids). Cathepsin A forms a complex with these two enzymes and directs their transport within the cell to the lysosomes. Within lysosomes, cathepsin A activates the enzymes and prevents their breakdown.