CTSA Mouse

Cathepsin-A Mouse Recombinant
Cat. No.
BT30295
Source
Sf9 Insect cells.
Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock
Quick Inquiry

Description

CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cathepsin-A (CTSA), also known as lysosomal protective protein, is essential for the stability and activity of lysosomal enzymes beta-galactosidase and neuraminidase. CTSA forms a complex with these enzymes and protects them from degradation. In addition to its protective role, CTSA exhibits carboxypeptidase activity and can deamidate tachykinins. Belonging to the peptidase S1 family, CTSA is localized in the lysosome as part of a multienzyme complex that includes beta-galactosidase and neuraminidase Neu1. CTSA is a multicatalytic enzyme possessing deamidase and esterase activities in addition to its carboxypeptidase function.
Description
Mouse CTSA, expressed in Sf9 Insect cells, is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) with a predicted molecular mass of 52.4 kDa. The recombinant protein appears as a band of approximately 50-70 kDa on SDS-PAGE due to glycosylation.
The CTSA protein is engineered with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile filtered colorless solution.
Formulation
The Mouse CTSA protein solution (0.5mg/ml) is supplied in phosphate buffered saline (pH 7.4) containing 10% glycerol.
Stability
Maintain stability by storing at 4°C for up to 2-4 weeks. For prolonged storage, freeze the product at -20°C.
Consider adding a carrier protein (0.1% HSA or BSA) for long-term storage.
Minimize freeze-thaw cycles to preserve protein integrity.
Purity
The purity of the Mouse CTSA protein is determined to be greater than 90.0% by SDS-PAGE analysis.
Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Source
Sf9 Insect cells.
Amino Acid Sequence
APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.

Product Science Overview

Functions and Activities

Cathepsin-A exhibits a variety of enzymatic activities depending on the pH environment:

  • Deaminidase and Esterase Activities: At neutral pH, Cathepsin-A expresses deaminidase and esterase activities .
  • Carboxypeptidase Activity: At acidic pH, it functions as a carboxypeptidase .

This enzyme is capable of hydrolyzing a range of bioactive peptide hormones, including endothelin and bradykinin, making it a promising target for therapeutic interventions in conditions such as heart failure .

Recombinant Mouse Cathepsin-A

The recombinant form of mouse Cathepsin-A is typically produced in a mouse myeloma cell line (NS0-derived). The recombinant protein includes a C-terminal 10-His tag for purification purposes . The molecular mass of the recombinant protein is approximately 53 kDa, although it may appear as 52-60 kDa under reducing conditions in SDS-PAGE due to post-translational modifications .

Purity and Activity

The recombinant mouse Cathepsin-A is highly purified, with a purity greater than 95% as determined by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining . The endotoxin level is less than 0.10 EU per 1 μg of the protein, as measured by the LAL method .

The specific activity of the recombinant enzyme is measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPPGFSAFK (Dnp)-OH. The specific activity is greater than 160 pmol/min/μg under the described conditions .

Storage and Stability

The recombinant mouse Cathepsin-A is supplied as a 0.2 μm filtered solution in Tris and NaCl. It is recommended to store the enzyme at -70°C to maintain its stability and avoid repeated freeze-thaw cycles . Under sterile conditions, the enzyme remains stable for up to 3 months after opening .

Applications

Recombinant mouse Cathepsin-A is used in various research applications, including:

  • Enzyme Activity Studies: To understand the enzymatic properties and substrate specificity.
  • Therapeutic Research: As a potential target for developing treatments for heart failure and other conditions involving bioactive peptide hormones .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.