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Cathepsin C from bovine spleen

Name: Cathepsin C from bovine spleen
Brand: SIGMA
Price: 251 USD
Availability: InStock

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

Synonym(s):

Dipeptidyl aminopeptidase, Dipeptidyl peptidase I

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Size/SKU	Availability	Price
10 units	Check Cart for Availability	$251.00
25 units	Check Cart for Availability	$423.00
100 units	Check Cart for Availability	$1,350.00

About This Item

CAS Number:

9032-68-2

EC Number:

3.4.14.1 (BRENDA, IUBMB)

UNSPSC Code:

12352204

EC Number:

232-881-4

NACRES:

NA.54

MDL number:

MFCD00081490

Specific activity:

≥5 units/mg protein

Assay:

>25% protein (biuret)

Biological source:

bovine spleen

Concentration:

≥5 unit/mg protein

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Properties

biological source

bovine spleen

Quality Segment

200

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

cow ... CTSC(352958)

Description

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

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.

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.

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.

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).

Physical form

Lyophilized from a 1 M sodium chloride solution.

Other Notes

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.

Disclaimer

Unstable. Keep frozen.

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This Item	A2580	A6778	HPA021282
Sigma-Aldrich C8511 Cathepsin C from bovine spleen	Sigma-Aldrich A2580 Angiotensin Converting Enzyme from porcine kidney	Sigma-Aldrich A6778 Angiotensin Converting Enzyme from rabbit lung	Sigma-Aldrich HPA021282 Anti-DPP7 antibody produced in rabbit
description Type X, lyophilized powder, ≥5 units/mg protein	description lyophilized powder, ≥10 units/mg protein (Bradford)	description ≥2.0 units/mg protein (modified Warburg-Christian)	description Prestige Antibodies^® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
assay >25% protein (biuret)	assay -	assay -	assay -
technique(s) activity assay: suitable	technique(s) -	technique(s) -	technique(s) immunofluorescence: 0.25-2 μg/mL, immunohistochemistry: 1:50-1:200, immunoblotting: 0.04-0.4 μg/mL
Gene Information cow ... CTSC(352958)	Gene Information pig ... ACE(613133)	Gene Information -	Gene Information human ... DPP7(29952)
specific activity ≥5 units/mg protein	specific activity ≥10 units/mg protein (Bradford)	specific activity ≥2.0 units/mg protein (modified Warburg-Christian)	specific activity -
biological source bovine spleen	biological source -	biological source -	biological source rabbit
suitability suitable for molecular biology	suitability -	suitability -	suitability -

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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