| Enzyme | Specificity |
Molecular Weight KDa | pH Optimum |
Extinction Coefficient E1%, 280nm | Common Substrates | Activators |
Inhibitors | Product Code/Applications |
|---|
Partially Purified for Tissue Dissociation and Protein Digestion |
| Collagenase | -Pro-X-†-Gly-Pro-Y-
X = neutral
Y = nonspecific |
68-130 | 6.3-7.5 |
13.20 (ColHG, Theoretical)
13.40 (ColHG, Theoretical) |
Collagen FALGPA Wünsch | Ca2+, Zn2+ |
alpha-2-macroglobulin Cysteine, histidine
DTT, 2-mercapto
EDTA, EGTA
Hg2+ & other heavy metal ions
ortho-phenanthroline |
Collagenase products
Tissue dissociation/ Primary cell isolation applications
(see Tissue Dissociation Guide for specific references). |
|---|
| Elastase | Elastin, -X-†-Y-
X = uncharged, nonaromatic
Y = nonspecific |
25.9 | 8.0-8.5 |
21.8 (Theoretical) |
Casein Denatured collagen Elastin, Fibrin Suc-Ala3-NA | None required |
alpha-antitrypsin
DFP
alpha-2-macroglobulin
PMSF |
ES/ESL, suspension/lyo powder
Tissue dissociation/ Primary cell isolation applications
(see Tissue Dissociation Guide for specific references). |
|---|
| Neutral Protease (Dispase®) | -X-†-Leu/Phe-†-Y-
X/Y = nonspecific |
36.0 | 5.9-7.0 |
13.96 (Theoretical) |
BAEE Casein | Ca2+, Mg2+, Mn2+, Fe2+,
and Al3+ |
EDTA, EGTA
Hg2+ & other heavy metal ions
ortho-phenanthroline |
NPRO/NPRO2
Tissue dissociation/ Primary cell isolation and cell harvesting applications
(see Tissue Dissociation Guide for specific references). |
|---|
| Papain | -X-†-Y-
X = nonspecific but Arg, Lys and
Phe preferred
Y = nonspecific |
23.0 | 6.0-7.0 |
22.88 (Theoretical) |
BAEE | Cysteine
EDTA
Reducing agents
GSH, NBS |
AEBSF, Antipain
Cystatin, Leupeptin
alpha-2-macroglobulin
Hg2+ & other heavy metal ions
DFP, PMSF
TLCK, TPCK, E-64 |
PAP/PAPL, suspension/lyo powder
Neural tissue dissociation/primary cell isolation applications
(see Tissue Dissociation Guide for specific references).
Antibody cleavage
RBC modification |
|---|
| Pepsin | -X-†-Y-
X = nonspecific but aromatic &
hydrophobic preferred
Y ≠ Ala, Gly, Val |
34.6 | 1.0-4.0
unstable ≥5 |
14.39
(Theoretical) |
Casein
Hemoglobin | None required |
Pepstatin A
Diazoketones
Epoxides |
PM
Collagen bioprocessing/purification
Antibody cleavage |
|---|
| Proteinase K | -X-†-Y-
X = nonspecific but
aliphatic, aromatic & hydrophobic preferred
Y = nonspecific |
28.9 | 7.5-12 |
8.23 (trypsinogen, theoretical)
8.69 (trypsin, theoretical)
37,000 (trypsin and trypsinogen, theoretical) |
Casein
Hemoglobin
Keratin | Ca2+
Active in 0.5-1% SDS |
DFP
EGTA
PMSF |
PROK, PROKS
DNA/RNA purification |
|---|
| Trypsin | -X-†-Y-
X = Arg, Lys
Y = nonspecific |
23.8 | 7.5-8.5 |
14.3 |
BAEE
Casein
TAME | Ca2+
Lanthanide |
Aprotinin, Benzamidine
DFP, EDTA, Leupeptin
alpha-2-macroglobulin
PMSF, TLCK
Trypsin Inhibitors (LBI, OI, SI/SIC) |
Trypsin products
Protein Digestion/Sequencing (purified)
Tissue dissociation/Primary cell isolation applications
(see Tissue Dissociation
Guide for specific references) |
|---|
Proteases for Protein Sequencing |
| Carboxy-peptidase B | H2-N-Rn-Y-†-X-COOH
X = basic
amino acids (Arg, Lys, Orn)
Y = nonspecific |
34.3 | 7.0-9.0 |
21.4 (Folk 1971) |
Hippuryl-L-arginine | None required |
EDTA
Hg2+ & other heavy metal ions
EDTA, EGTA ortho-phenanthroline |
COBC/COBPMS
Sequence analysis by successive cleavage of C-terminal basic amino
acids Insulin production |
|---|
| Carboxy-peptidase Y | H2-N-Rn-Y-†-X-COOH
X,Y = nonspecific |
64.0 | 4.5-6.0 |
15.0
(Hayashi et al. 1973, and Kuhn et al. 1973) |
ATEE
Bz-Phe-Ala-Leu
Z-Phe-Ala | None required |
APCK, Aprotinin
DFP
4-Hydroxymercuribenzoate
PMSF |
COY
C-terminal sequencing & Modification/labeling of peptides and proteins |
|---|
| Chymotrypsin TLCK treated | -X-†-Y-
X = aromatic
Y = nonspecific |
25.6 | 7.8-8.0 |
20.57
(Theoretical) |
ATEE
BTEE | Ca2+ |
alpha-antitrypsin
Aprotinin
DFP, PMSF, TPCK
alpha-2-macroglobulin |
CDSEQ/CDTLCK
Sequence analysis
Peptide synthesis, mapping/fingerprinting |
|---|
Endo-Arg-C
(Clostripain) | -Arg-†-Y-
Y = nonspecific |
53 | 7.4-7.8 |
16.57
(Theoretical) |
BAEE | Ca2+
Reducing agents |
EDTA, TLCK, Tris
Hg2+ & other heavy metal ions |
CPSEQ, CP
Peptide mapping & synthesis
Sequence analysis
Hydrolysis/condensation of amide bonds |
|---|
| Endo-Glu-C (Staph. Protease V8) | -Glu-†-Y-
(NH4 buffers pH 4, 7.8)
-Asp-†-Y-
(PO4 buffer pH 7.8) |
27.0 | 4.0 & 7.8 |
4.26
(Houmard 1976) |
Casein
Z-Phe-Leu-Glu-4NA | None required |
DFP
F-, Cl-, Br-, CH3COO-
NO3-
alpha-2-macroglobulin |
STSEQ, STAP
Peptide mapping & sequence analysis |
|---|
| SequENZ™ Trypsin, Sequencing Grade, Modified |
-X-†-Y-
X = Arg, Lys
Y = nonspecific |
23.8 |
7.5-8.5 |
14.3 |
BAEE
Casein
TAME |
Ca2+
Lanthanide |
Aprotinin, Benzamidine
DFP, EDTA, Leupeptin
alpha-2-macroglobulin-
PMSF, TLCK
Trypsin Inhibitors (egg white, lima bean, pancreatic, soybean) |
TRSEQZ, Modified Sequencing Grade
chemically modified to reduce autolysis
Peptide mapping & sequence analysis
Cleavage fusion proteins |
|---|
| Trypsin, Sequencing Grade, Native |
TRSEQII, Sequencing Grade, Native
Peptide mapping & sequence analysis
Cleavage fusion proteins |
|---|
| Trypsin, TPCK Treated |
TRTPCK, TPCK Treated
Peptide mapping & sequence analysis
Cleavage fusion proteins |
|---|
Place Order