Analytical Data
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Gene name
Cathepsin A
- Application
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Alternative Names
CTS-A; GLB2; GSL; NGBE; PPCA; PPGB; Protective Protein For Beta-Galactosidase; Galactosialidosis; Carboxypeptidase C; Carboxypeptidase L
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P16675
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Expression Region
Gly200~Val435
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Molecular Weight
57kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Cathepsin A (Cat A), a member of the cathepsin family of cysteine proteases, plays a significant role in various physiological processes, including protein catabolism and antigen processing. Its dysfunction is associated with several pathological conditions, including lysosomal storage diseases and certain types of cancer. The study of recombinant Cathepsin A has gained attention due to its potential in therapeutic applications and as a target for drug development. By producing recombinant forms of this protein, researchers aim to elucidate its structure-function relationships, improve our understanding of its enzymatic mechanisms, and develop specific inhibitors or modulators that can be used in clinical settings. Furthermore, recombinant Cathepsin A can be utilized in biochemical assays to study its substrate specificity and activity under varying physiological conditions, providing insights into its role in health and disease. As research continues to reveal the complexities of Cat A's interactions within cellular environments, the development of recombinant proteins presents a valuable approach to explore its biological significance and therapeutic potential.
