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Recombinant Human Cathepsin C Protein (His Tag)

Cat No.: BLPSN-0599
CPPI Protein, Human; DPP-I Protein, Human; DPP1 Protein, Human; DPPI Protein, Human; HMS Protein, Human; JP Protein, Human; JPD Protein, Human; PALS Protein, Human; PDON1 Protein, Human; PLS Protein, Human
tag His
host species Human
accession NP_001805.3
background Cathepsins are proteases found in many types of cells conserved in all animals, which have a vital role in mammalian cellular turnover such as bone resorption. The lysosomal cysteine protease Cathepsin C (CTSC), also known as dipeptidyl peptidase I (DPPI/DPP1), activates a number of granule-associated serine proteases with pro-inflammatory and immune functions by removal of their inhibitory N-terminal dipeptides. This lysosomal exo-cysteine protease belonging to the peptidase C1 family. Active cathepsin C is found in lysosomes as a 2-kDa multimeric enzyme. Subunits constituting this assembly all arise from the proteolytic cleavage of a single precursor giving rise to three peptides: the propeptide, the alpha- and the beta-chains. It is a central coordinator for activation of many serine proteases in immune/inflammatory cells. Defects in the Cathepsin C have been shown to be a cause of Papillon-Lefevre disease, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Cathepsin C plays a key role in the activation of several degradative enzymes linked to tissue destruction in inflammatory diseases. Thus, it is a therapeutic target for the treatment of a number of inflammatory and autoimmune diseases.
description A DNA sequence encoding the pro form of human cathepsin C (NP_001805.3) (Met 1-Leu 463) was expressed with a His tag at the C-terminus.
source HEK293
predicted n terminal Asp 25
AA sequence Met 1-Leu 463
molecular weight The secreted recombinant human cathepsin C exists as the pro form after removal of the signal peptide. It consists of 450 a.a. and has a predicted molecular mass of 51 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhCTSC is approximately 55 kDa.
purity >92% as determined by SDS-PAGE
endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
bioactivity Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Arg-7-amido-4-methylcoumarin (GRAMC). The specific activity is >200 pmoles/min/ug.(Activation description: The proenzyme needs to be activated by Cathepsin L for an activated form)
formulation Lyophilized from sterile PBS, pH 7.4.
stability The recombinant proteins are stable for up to 1 year from date of receipt at -70℃.
usage For Research Use Only
storage Store the protein 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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