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Recombinant Human Cathepsin A/Lysosom Carboxypeptidase A, CF

Catalog # 1049-SE | R&D Systems, Inc. a Bio-Techne Brand
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1049-SE-010

Key Product Details

Source

NS0

Accession #

Structure / Form

Pro form

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human Cathepsin A/Lysosomal Carboxypeptidase A protein
Ala29-Tyr480, with a C-terminal 10-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ala29

Predicted Molecular Mass

53 kDa

SDS-PAGE

51-62 kDa, reducing conditions

Activity

Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPPGFSAFK(Dnp)-OH (Catalog # ES005).
The specific activity is >75 pmol/min/µg, as measured under the described conditions.

Formulation, Preparation and Storage

1049-SE
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Cathepsin A/Lysosomal Carboxypeptidase A

Cathepsin A/lyososomal carboxypeptidase A is a member of the serine carboxypeptidase family (1). Cathepsin A is a multifunctional enzyme that expresses deaminidase and esterase activities at neutral pH and carboxypeptidase activity at acidic pH. Also known as protective protein, its association with beta-galactosidase ( beta-gal) and neuraminidase is essential for beta-gal stability and neuraminidase activation in the lysosomes. Inherited deficiency of Cathepsin A causes the lysosomal storage disorder galactosialidosis, characterized by a combined secondary deficiency of beta-gal and neuraminidase. Cathepsin A is capable of hydrolyzing a variety of bioactive peptide hormones including tachykinins, indicating that extralysosomal Cathepsin A plays a role in regulation of functions of these molecules (2). Cathepsin A is synthesized as a single-chain precursor and processed into heavy (32 kDa) and light (20 kDa) chains, which are linked by disulfide bonds.

References

  1. Pshezhetsky, A.V. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, A.J. et al.) p. 1923, Academic Press, San Diego.
  2. Hiraiwa, M. (1999) Cell. Mol. Life. Sci. 56:894.

Alternate Names

CTSA, Lysosomal Carboxypeptidase A

Entrez Gene IDs

5476 (Human); 19025 (Mouse)

Gene Symbol

CTSA

UniProt

Product Documents for Recombinant Human Cathepsin A/Lysosom Carboxypeptidase A, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Cathepsin A/Lysosom Carboxypeptidase A, CF

For research use only

Citations for Recombinant Human Cathepsin A/Lysosom Carboxypeptidase A, CF (4)

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FAQs for Recombinant Human Cathepsin A/Lysosom Carboxypeptidase A, CF

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  • Q: Where does Cathepsin A cleave Mca-RPPGFSAFK(Dnp)-OH Fluorogenic Peptide Substrate, Catalog # ES005?

    A: Although the QC assay conditions provided on our recombinant Cathepsin A datasheets should favor carboxypeptidase activity, it is possible that there is more than one site in the ES005 peptide recognized and cleaved by Cathepsin A.  We have not performed verification experiments to confirm the cleavage site preferred in our reaction conditions.

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