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C8511

Sigma-Aldrich

Cathepsin C from bovine spleen

Type X, lyophilized powder, ≥5 units/mg protein

Synonym(s):

Dipeptidyl aminopeptidase, Dipeptidyl peptidase I

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine spleen

type

Type X

Assay

>25% protein (biuret)

form

lyophilized powder

specific activity

≥5 units/mg protein

composition

Protein, ≥25% biuret

manufacturer/tradename

Sigma-Aldrich

storage condition

OK to freeze (Unstable. Keep frozen)

concentration

≥5 unit/mg protein

technique(s)

activity assay: suitable

suitability

suitable for molecular biology

application(s)

life science and biopharma

shipped in

dry ice

storage temp.

−20°C

Gene Information

General description

Research Area: Cell Signaling
Dipeptidyl peptidase I (DPPI), also known as cathepsin C, is an abundant lysosomal cysteine protease from the papain superfamily with a molecular weight of approximately 200 kDa. It is widely expressed in a variety of mammalian tissues, with the highest levels found in the lungs, kidneys, liver, and spleen, and relatively lower levels in the brain.
DPPI is the only member of its family that is functional as a tetramer, consisting of four identical subunits, each composed of an N-terminal fragment, a heavy chain, and a light chain. It is identified as one of the multifaceted protease-processing machines, having been shown to function beyond its role as a non-specific lysosomal protease.

Application

Cathepsin C from bovine spleen has been used for the in vitro enzyme activity assays. It has also been used as a digestion enzyme for in vitro myelin oligodendrocyte glycoprotein (MOG) digestion.
Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels.
The enzyme from Sigma has been used in the activation of granzyme k (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions.

Biochem/physiol Actions

Cathepsin C (Cat C) serves as the physiological activator of groups of serine proteases within immune and inflammatory cells, playing a crucial role in the defense mechanisms of an organism. It may play a role in chronic airway diseases such as asthma. Cat C also acts as a protease link between inflammation and thrombosis.
Cat C participates in neutrophil recruitment and production of chemokines and cytokines in many inflammatory diseases. Cathepsin C plays a crucial role as an essential enzyme in activating granule serine proteases in cytotoxic T lymphocytes, natural killer cells (granzymes A and B), mast cells (chymase and tryptase), and neutrophils (cathepsin G, proteinase 3, and elastase).
Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators.

Caution

Unstable. Keep frozen.

Unit Definition

One unit will produce 1 μmole of Gly-Phe-NHOH from Gly-Phe-NH2 and hydroxylamine per min at pH 6.8 at 37 °C using DL-phenylalanine hydroxamic acid as the standard. In addition to its hydrolytic properties, cathepsin C catalyzes the polymerization of dipeptide amides.

Physical form

Lyophilized from a 1 M sodium chloride solution.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Up-regulation of microglial cathepsin C expression and activity in lipopolysaccharide-induced neuroinflammation
Fan K, et al.
Journal of Neuroinflammation, 9, 1-13 (2012)
Case of rippled-pattern sebaceoma with clinically yellowish surface and histopathological paucity of lipid-containing neoplastic cells.
Yoshio Kawakami et al.
The Journal of dermatology, 39(7), 644-646 (2011-11-15)
Mayumi Ueta et al.
Japanese journal of ophthalmology, 55(4), 405-410 (2011-05-28)
We previously reported that human conjunctival epithelial cells expressed functioning interleukin-4 receptor α (IL-4Rα). In this study, we investigated whether human corneal epithelial cells also express functioning IL-4Rα. The presence of IL-4Rα mRNA and protein in human corneal epithelium was
ClC-7 drives intraphagosomal chloride accumulation to support hydrolase activity and phagosome resolution
Wu JZ, et al.
The Journal of cell biology, 222(6), e202208155-e202208155 (2023)
Christian D Sadik et al.
Clinical oral investigations, 16(2), 591-597 (2011-03-08)
Papillon-Lefèvre syndrome (PLS) is characterised by aggressively progressive periodontitis combined with palmo-plantar hyperkeratosis. It is caused by "loss of function" mutations in the cathepsin C gene. The hypothesis behind this study is that PLS patients' polymorphonuclear leukocytes (PMNs) produce more

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