CTSC Mouse

Cathepsin-C Mouse Recombinant
Cat. No.
BT30432
Source

HEK293 cells.

Synonyms

DPPI, Cathepsin C, CTSC

Appearance
Sterile Filtered clear solution.
Purity

Greater than 95% 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

Description

CTSC Mouse Recombinant produced in HEK293 cells is a single, polypeptide chain containing 444 amino acids (25-462 a.a.) and having a molecular mass of 50.5kDa. CTSC is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

Cathepsin C (CTSC) is a key enzyme involved in the activation of serine proteases found in granules within inflammatory cells. It specifically cleaves dipeptides from the N-terminal end of protein and peptide substrates. The activation of these proteases by CTSC enables them to break down components of the extracellular matrix. This process, while important for normal physiological functions, can contribute to tissue damage and chronic inflammation if not properly regulated. CTSC is a tetrameric enzyme, meaning it is composed of four subunits. Each subunit consists of three parts: an N-terminal proregion fragment, a heavy chain, and a light chain. Defects in the CTSC gene can lead to Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by severe periodontal disease.

Description

Recombinant CTSC protein derived from mouse has been produced in HEK293 cells. This protein is a single polypeptide chain consisting of 444 amino acids (amino acids 25-462), resulting in a molecular weight of 50.5 kDa. A 6-amino acid Histidine tag is present at the C-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.

Physical Appearance
Clear, sterile solution after filtration.
Formulation

The CTSC protein is supplied in a solution with a concentration of 0.5 mg/ml. The solution contains Phosphate Buffered Saline at a pH of 7.4 and 10% glycerol.

Stability
For optimal storage, keep the vial at 4°C if it will be used within 2-4 weeks. For longer storage, freeze the protein at -20°C. To ensure stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). It's important to avoid repeated freeze-thaw cycles.
Purity

The purity of the protein is greater than 95% as determined by SDS-PAGE analysis.

Biological Activity

The enzyme exhibits significant biological activity, exceeding 50,000 pmol/min/ug. This activity is measured as the amount of enzyme required to hydrolyze 1 picomole of GlyArg-AMC per minute at a pH of 6.0 and a temperature of 37°C.

Synonyms

DPPI, Cathepsin C, CTSC

Source

HEK293 cells.

Amino Acid Sequence

DTPANCTYPD LLGTWVFQVG PRSSRSDINC SVMEATEEKV VVHLKKLDTA YDELGNSGHF TLIYNQGFEI VLNDYKWFAF FKYEVRGHTA ISYCHETMTG WVHDVLGRNW ACFVGKKVES HIEKVNMNAA HLGGLQERYS ERLYTHNHNF VKAINTVQKS WTATAYKEYE KMSLRDLIRR SGHSQRIPRP KPAPMTDEIQ QQILNLPESW DWRNVQGVNY VSPVRNQESC GSCYSFASMG MLEARIRILT NNSQTPILSP QEVVSCSPYA QGCDGGFPYL IAGKYAQDFG VVEESCFPYT AKDSPCKPRE NCLRYYSSDY YYVGGFYGGC NEALMKLELV KHGPMAVAFE VHDDFLHYHS GIYHHTGLSD PFNPFELTNH AVLLVGYGRD PVTGIEYWII KNSWGSNWGE SGYFRIRRGT DECAIESIAV AAIPIPKL-HHHHHH

Product Science Overview

Introduction

Cathepsin C (CTSC), also known as dipeptidyl peptidase I (DPPI), is a lysosomal cysteine protease belonging to the papain-like cysteine peptidases family . It plays a crucial role in the immune system by activating various serine proteases, which are essential for immune defenses, antimicrobial activity, inflammation, and programmed cell death (apoptosis) . Recombinant mouse Cathepsin C is a valuable tool for studying these processes in a controlled laboratory setting.

Structure and Function

Cathepsin C is a tetrameric enzyme composed of four identical subunits, each containing a heavy chain, a light chain, and an exclusion domain . The enzyme sequentially removes dipeptides from the free N-termini of proteins and peptides, except when a basic amino acid (Arg or Lys) is in the N-terminal position or Pro is on either side of the scissile bond . This broad specificity allows Cathepsin C to participate in various physiological processes.

Expression and Activation

Cathepsin C is constitutively expressed at high levels in the lung, kidney, liver, and spleen . It is synthesized as an inactive proenzyme (zymogen) and undergoes proteolytic cleavage to become active . In the laboratory, recombinant mouse Cathepsin C is typically produced using a mouse myeloma cell line (NS0) and activated by recombinant human Cathepsin L .

Role in Health and Disease

Cathepsin C is pivotal in activating serine proteases in cytotoxic T cells, natural killer cells, mast cells, and neutrophils . These proteases include granzymes A and B, chymase, tryptase, cathepsin G, neutrophil elastase, and proteinase 3 . Dysregulation of Cathepsin C is linked to various inflammatory diseases, such as chronic obstructive pulmonary disease (COPD), asthma, cystic fibrosis, and COVID-19-related acute respiratory distress syndrome (ARDS) . Additionally, mutations in the CTSC gene are associated with genetic disorders like Papillon–Lefevre syndrome (PLS), Haim–Munk syndrome (HMS), and aggressive periodontitis (AP) .

Therapeutic Potential

Given its central role in immune and inflammatory responses, Cathepsin C is being explored as a potential therapeutic target for autoimmune and inflammatory disorders . Inhibitors of Cathepsin C could potentially mitigate the excessive inflammation and tissue damage observed in these conditions.

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