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C8511

Sigma-Aldrich

Cathepsin C from bovine spleen

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

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Synonym(s):
Dipeptidyl aminopeptidase, Dipeptidyl peptidase I
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

type

Type X

form

lyophilized powder

specific activity

≥5 units/mg protein

composition

Protein, ≥25% biuret

shipped in

dry ice

storage temp.

−20°C

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This Item
C9584C3888A2580
specific activity

≥5 units/mg protein

specific activity

≥125 units/mg protein

specific activity

≥50 units/mg protein

specific activity

≥10 units/mg protein (Bradford)

shipped in

dry ice

shipped in

-

shipped in

wet ice

shipped in

dry ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

type

Type X

type

-

type

-

type

-

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.

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

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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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