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MilliporeSigma

C8511

Sigma-Aldrich

Cathepsin C from bovine spleen

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

Sinónimos:

Dipeptidyl aminopeptidase, Dipeptidyl peptidase I

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type X

Quality Level

form

lyophilized powder

specific activity

≥5 units/mg protein

composition

Protein, ≥25% biuret

shipped in

dry ice

storage temp.

−20°C

Categorías relacionadas

Application

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

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.

substrate

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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The specificity of dipeptidyl transferase.
I M Voynick et al.
Biochemistry, 7(1), 40-44 (1968-01-01)
H Lindley
The Biochemical journal, 126(3), 683-685 (1972-02-01)
1. The characterization of cathepsin C as an aminodipeptidase has been confirmed. 2. An extra limitation on its specificity, namely that peptides involving proline as the third residue are immune to the enzyme, has been found. 3. A novel technique
High immunoglobulin E in a Chinese Papillon-Lefèvre syndrome patient with novel compound mutations of cathepsin C.
Xuan Wen et al.
The Journal of dermatology, 39(7), 664-665 (2012-01-10)
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

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