PROTEASOMES AND PROTEASES
(SEE APOPTOSIS SECTION FOR CPP32 AND ICE PROTEASE REAGENTS)
PROTEASOME INHIBITORS
PI-102
MG-132
Z-Leu-Leu-Leu-CHO
98%, MW=475.6 [133407-82-6] Storage: -20°C
A potent and selective reversible proteasome inhibitor (Ki= 4 nM). Inhibits NF-kB activation by preventing IkB
degradation (IC50=3 mM)1.
5 mg
5 x 5 mg
PI-104
Lactacystin
99%, MW=376.4 [133343-34-7] Storage: -20°C
A potent and selective irreversible proteasome inhibitor2.
Inhibits NF-kB activation by inhibiting IkB
degradation (IC50=10 mM)3.
Induces neurite outgrowth in Neuro 2A mouse neuroblastoma cells4.
200 µg
5 x 200 µg
CALPAIN
CALPAIN INHIBITORS
P-120
Calpain Inhibitor I (ALLN)
N-Acetyl-Leu-Leu-Nle-CHO
>97%, MW=383.5, Storage: -20°C
Cell-permeable, peptide aldehyde inhibitor of calpain and other neutral cysteine
proteases. Inhibits cell cycle progression at G1/S and metaphase/anaphase in CHO cells by
inhibiting cyclin B degradation5. Also stimulates HMG-CoA
synthase transcription by inhibiting degradation of active SREBP-1 (sterol regulatory
element-binding protein 1)6. Inhibits proteolytic degradation
of IkBa and IkBb in RAW macrophages induced with LPS7.
5 mg
25 mg
PI-100
Calpain Inhibitor II (ALLM)
N-Acetyl-Leu-Leu-Met-CHO
98%, MW=401.6 [136632-32-1] Storage: -20°C
Cell-permeable, peptide aldehyde inhibitor of calpain and other neutral cysteine
proteases. Potent inhibitor of cathepsin L (Ki=0.6 nM) and cathepsin B (Ki=100
nM)9.
5 mg
25 mg
PI-101
Calpeptin
Z-Leu-Nle-CHO
(N-Benzyloxycarbonyl-L-leucylnorleucinal)
98%, MW=362.5, Storage: -20°C
Cell-permeable, peptide aldehyde inhibitor of calpain and other neutral cysteine
proteases. Inhibits calpain8 and cathepsin L9,10.
10 mg
50 mg
PI-105
E-64
trans-Epoxy succinyl-L-leucylamido-(4-guanidino) butane
98%, MW=357.4 [66701-25-5] Storage: -20°C
Cell-permeable, epoxysuccinyl peptide irreversible inhibitor of calpain and other cysteine
proteases11,14. Inhibits a calpain-dependent apoptosis
pathway in T cells12 but promotes heat-induced apoptosis in
FM3A cells13.
5 mg
25 mg
PI-106
E-64-c
(2S,3S)-trans-Epoxysuccinyl-L-leucylamido-3-methylbutane
98%, MW=314.4 [76684-89-4] Storage: -20°C
Cell-impermeable epoxysuccinyl peptide inhibitor of calpain and other cysteine proteases11. Inhibits calpain and cathepsin B, H and L14.
1 mg
5 mg
PI-107
E-64-d
(2S,3S)-trans-Epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester
98%, MW=342.4 [88321-09-9] Storage: -20°C
Cell-permeable, ethyl ester of E-64-c, above. The ester is hydrolyzed by intracellular
esterases to produce E-64-c. Inhibits calpain and cathepsin B, H and L15,16.
1 mg
5 mg
CALPAIN ANTIBODIES
SA-256
Anti-?Calpain (calpain I), domain II
Mouse monoclonal antibody. Clone 2H2A7C2. Immunogen: Purified bovine skeletal muscle
?calpain17. Supplied as ascites IgG1. Epitope is in large
subunit, catalytic domain II of human ?calpain (residues 245-265). Recognizes human,
bovine and rat 80 kDa subunit of ?calpain. Applications: WB 1/1000, IF 1/25.
100 µl
SA-257
Anti-?Calpain (calpain I), domain III
Mouse monoclonal antibody. Clone 9A4H8D3. Immunogen: Purified bovine skeletal muscle
?calpain17. Supplied as ascites IgG1. Epitope is in large
subunit, domain III of human ?calpain (residues 465-520). Recognizes 80 kDa subunit of
?calpain from several mammalian species. Applications: WB 1/2000, IF 1/100.
100 µl
SA-255
Anti-m-Calpain (calpain II)
Mouse monoclonal antibody. Clone 107-82. Immunogen: Purified bovine skeletal muscle
m-calpain17. Supplied as ascites IgG1. Epitope is in large
subunit, domain III/IV of human calpain (residues 502-699). Recognizes human, procine and
rat 80 kDa subunit of m-calpain. Applications: WB 1/500, IF 1/50.
100 µl
SA-283
Anti-Calpastatin, domain II
Mouse monoclonal antibody. Clone 2G11D6. Immunogen: Purified bovine skeletal muscle
calpastatin17. Supplied as ascites IgG2a. Epitope is in
domain II of human calpastatin (residues 295-501). Recognizes ~77 kDa human, bovine and
rat calpastatin. Western blotting shows 150, 125, 90 and 70 kDa protein bands believed to
be translation variants of calpastatin. Applications: WB 1/5000, IF 1/1000.
100 µl
SA-284
Anti-Calpastatin, domain IV
Mouse monoclonal antibody. Clone 1F7E3D10. Immunogen: Purified bovine skeletal muscle
calpastatin17. Supplied as ascites IgG1. Epitope is in
domain IV of human calpastatin (residues 543-673). Recognizes ~77 kDa human, bovine and
rat calpastatin. Western blotting shows 150, 125, 90 and 70 kDa protein bands believed to
be translation variants of calpastatin. Applications: WB 1/5000, IF 1/200.
100 µl
OTHER PROTEASE INHIBITORS
EI-212
Bestatin (Ubenimex)
99%, MW=308.4 [65391-42-6] Storage: 0°C
Aminopeptidase inhibitor18, Ki=3.5 µM for
aminopeptidase-M19. Inhibits LTA4 hydrolase, a
dual function protease and epoxide hydrolase, in a rapid, reversible, dose-dependent
manner (IC50=4 µM)20. Immunomodulator21.
5 mg
25 mg
EI-213
Captopril
99%, MW=217.3 [62571-86-2] Storage: RT
Reversible and competitive inhibitor of LTA4 hydrolase (IC50=11 µM)22. An orally active inhibitor of angiotensin converting enzyme
(ACE)20.
1 g
5 g
REFERENCES
1. J. Adams and R. Stein Ann. Rep. Med. Chem. 1996 31 279
2. G. Fenteany et al. Science 1995 268 726
3. L.R. Dick et al. J. Biol. Chem. 1997 272 182
4. G. Fenteany et al. Proc. Natl. Acad. Sci. USA 1994 91 3358
5. S.W. Sherwood et al. Proc. Natl. Acad. Sci. USA 1993 90 3353
6. X. Wang et al. Cell 1994 77 53
7. S.A. Milligan et al. Arch. Biochem. Biophys. 1996 335 388
8. Y. Banno et al. J. Biol. Chem. 1995 270 4318
9. T. Sasaki et al. J. Enz. Inhib. 1990 3 195
10. Tsujinaka et al. Biochem. Biophys. Res. Commun. 1988 153 1201
11. K.K.W. Wang and P.-W. Yuen TIPS 1994 15 411
12. A. Sarin et al. J. Immunol. 1994 153 862
13. W.G. Zhu et al. Biochem. Biophys. Res. Commun. 1996 225 924
14. A.J. Barrett et al. Biochem. J. 1982 201 189
15. M. Tamai et al. Chem. Pharm. Bull. 1987 35 1098
16. E.B. McGowan et al. Biochem. Biophys. Res. Commun. 1989 158 432
17. J. Cong et al. J. Biol. Chem. 1993 268 25740
18. S. Wilkes and J. Prescott J. Biol. Chem. 1985 260 13154
19. C. Tarnus et al. Bioorg. Med. Chem. 1996 4 1287
20. L. Orning et al. J. Biol. Chem. 1991 266 1375
21. V. St Georgiev Trends Pharmacol. Sci. 1990 11 373
22. L. Orning et al. J. Biol. Chem. 1991 266 16507
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