Download Protease Proteins

Protease Proteins
Products currently
available from PeproTech:
Products
Catalogue#
Aeromonas Aminopeptidase . .........100-10
Human Enterokinase ................... 450-48C
Human MMP-1 ..............................420-01
Human MMP-2 ..............................420-02
Human MMP-3 ..............................420-03
Murine Granzyme B .......................140-03
Rat Carboxypeptidase-B .................400-00
Staphylococcus Glu-C ....................450-46
Yeast Kex-2 . ...................................450-45
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The role of Protease Proteins:
Proteases (also called Proteolytic Enzymes,
Peptidases, or Proteinases) are enzymes
that hydrolyze the amide bonds within
proteins or peptides. Most proteases act in
a specific manner, hydrolyzing bonds at or
adjacent to specific residues or a specific
sequence of residues contained within the
substrate protein or peptide. Proteases play
an important role in most diseases and
biological processes including prenatal and
postnatal development, reproduction, signal
transduction, the immune response, various
autoimmune and degenerative diseases, and
cancer. They are also an important research
tool, frequently used in the analysis and
production of proteins.
Graphical structural depiction of the
MMP-1 protein
Proteins relevant for Protease Research:
Protease Proteins:
PeproTech’s protease products are fully purified recombinant
proteins, which are free from any contaminating proteins or
activities that could yield ambiguous results or otherwise
complicate analyses. These products are fully tested for
activity and specificity and most are produced by an animalfree process.
Yeast Kex-2
Synonyms: Endoproteinase Lys/Arg-Arg
Description: Kex-2 cleaves at the carboxyl side of
the recognition sequence, (K/R) - R.
Recombinant Yeast Kex-2 is a 59.9 kDa
protease consisting of 554 amino acid
residues.
Staphylococcus Glu-C
Synonyms: V8 Protease
Description: Glu-C cleaves at the Carboxyl side of E (can
also cleave D under certain conditions).
Recombinant Staphylococcus Glu-C is a
28.8 kDa protease consisting of 266 amino
acid residues.
Murine Granzyme B
Synonyms: none
Description: Granzyme B is a cysteine protease found
in the cytoplasmic granules of cytolytic
T lymphocytes (CTL) and natural killer
(NK) cells. Granzyme B is required for the
induction of target cell lysis, which occurs as
part of cell mediated immune responses, and
can activate apoptosis in target cells by both
caspase dependent and caspase independent
mechanisms. Proteolytic cleavage of substrates
by Granzyme B takes place primarily after
aspartic acid residues. Recombinant murine
Granzyme B is a glycosylated 227 amino acid
protein, comprising the mature active portion
of the murine Granzyme B precursor. The
apparent molecular weight is 28.9 kDa by
mass spectrometry.
Continued…
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18/3//2010
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Proteins relevant for Protease Research continued
Human Enterokinase
Aeromonas Aminopeptidase
Synonyms: none
Description: Enterokinase cleaves at the carboxyl side
of the recognition sequence D-D-D-D-K.
Human Enterokinase is expressed as a linear
1019 amino acid polypeptide precursor
glycoprotein. Proteolytic processing of this
precursor generates the biologically active
form of Enterokinase, which consists of two
polypeptide chains (heavy chain and light
chain) held together by a single disulfide
bond, resulting in formation of a biologically
active heterodimer. The heavy chain consists
of 784 amino acid residues, and the light
consists of 235 amino acid residues.
Rat Carboxypeptidase-B
Synonyms: none
Description: Sequentially cleaves N-terminal amino
acids except E, D, and X-P. Recombinant
Aeromonas Aminopeptidase is a 31.4 kDa
protein containing 291 amino acid residues.
Synonyms: none
Description: Carboxypeptidase-B sequentially cleaves C
terminal K and R residues.
MMP Proteins:
The role of MMP’s: Matrix metalloproteinases (MMPs)
are a family of endoproteases that require zinc and calcium
for expressing catalytic activity. These enzymes play a central
role in the maintenance and remodeling of the extracellular
matrix. Elevated expression of their activity, caused either by
up-regulation of their expression or down-regulation of their
cognate inhibitors, has been implicated in various degenerative
disorders, including arthritis, cardiovascular disease, skeletal
growth-plate disorders, and cancer metastasis.
Human MMP-1
Synonyms: Matrix metalloproteinase-1; Fibroblast collagenase; interstitial collagenase
Description: MMP-1 is a secreted collagenase with
specificity toward Type I, II, III, VII, and X
collagens. Recombinant human MMP-1 is a
42.7 kDa protein containing the entire catalytic
domain and the C-terminal domain, which is
involved in substrate specificity and binding
TIMP-1 (371 amino acids).
Human MMP-2
Synonyms: Matrix metalloproteinase-2; Gelatinase A,
TBE-1
Description: MMP-2 is a secreted collagenase with
specificity toward Type IV, V, VII, and X
collagens. Recombinant human MMP-2 is a
62.0 kDa protein containing the entire catalytic
domain and the C-terminal domain, (552
amino acids).
MMP-1 activity was measured by its ability to cleave a chromogenic
peptide MMP-1 substrate at room temperature. Using MMP-1 at
a concentration of 2.5 mg/ml, 50% cleavage was achieved at an
incubation time of approximately 25 minutes.
Human MMP-3
Synonyms: Stromelysin-1, SL-1, Transin-1
Description: MMP-3 degrades fibronectin, laminin, collagens
III, IV, and X, and cartilage proteoglycans.
Recombinant human MMP-3 is a 42.8 kDa
protein containing the entire catalytic domain
and the C-terminal domain (378 amino
acids).