C8176
Collagenase from Clostridium histolyticum
Sigma Blend Type L, ≤1.0 FALGPA units/mg solid
Synonym(s):
Clostridiopeptidase A
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-582-9
MDL number:
Specific activity:
≤1.0 FALGPA units/mg solid
Pricing and availability is not currently available.
Quality Level
form
powder
caseinase activity
≥40 units/mg solid
specific activity
≤1.0 FALGPA units/mg solid
mol wt
68-130 kDa
storage temp.
−20°C
Application
Collagenase from Clostridium histolyticum, or Clostridiopeptidase A, has been used in a study to assess the synthesis and in vitro evaluation of macromolecular antitumour derivatives based on phenylenediamine mustard. Clostridiopeptidase A has also been used in a study to investigate the enzymatic debridement of burn wounds with collagenase.
Biochem/physiol Actions
Collagenase is activated by four gram atom calcium per mole enzyme. It is inhibited by ethylene glycol-bis(beta-aminoethyl ether) - N, N, N′,N′-tetraacetic acid, beta-mercaptoethanol, glutathione, thioglycolic acid and 8-hydroxyquinoline.
Effective release of cells from tissue requires the action of collagenase enzymes and the neutral protease. Collagenase is activated by four gram atom calcium (Ca2+) per mole enzyme. The culture filtrate is thought to contain at least 7 different proteases ranging in molecular weight from 68-130 kDa. The pH optimum is 6.3-8.8. The enzyme is typically used to digest the connective components in tissue samples to liberate individual cells. Ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA)4; β-mercaptoethanol; glutathione, reduced; thioglycolic acid, sodium; and 2,2′-dipyridyl; 8-hydroxyquinoline are known to inhibit the enzyme activity.
Other Notes
One collagen digestion unit (CDU) liberates peptides from collagen from bovine achilles tendon equivalent in ninhydrin color to 1.0 μmole of leucine in 5 hours at pH 7.4 at 37 °C in the presence of calcium ions. One FALGPA hydrolysis unit hydrolyzes 1.0 μmole of furylacryloyl-Leu-Gly-Pro-Ala per min at 25°C. One Neutral Protease unit hydrolyzes casein to produce color equivalent to 1.0 μmole of tyrosine per 5 hr at pH 7.5 at 37°C. One Clostripain Unit hydrolyzes 1.0 μmole of BAEE per min at pH 7.6 at 25°C in the presence of DTT.
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This Item | |||
|---|---|---|---|
| specific activity ≤1.0 FALGPA units/mg solid | specific activity ≥1.0 FALGPA units/mg solid | specific activity ≥1 FALGPA units/mg solid, ≥125 CDU/mg solid | specific activity ≥800 CDU/mg solid, 2-5 FALGPA units/mg solid |
| form powder | form powder | form lyophilized powder | form powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| mol wt 68-130 kDa | mol wt 68-130 kDa | mol wt 68-125 kDa | mol wt 68-130 kDa |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| caseinase activity ≥40 units/mg solid | caseinase activity ≥10 units/mg solid | caseinase activity - | caseinase activity - |
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signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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N I Solov'eva et al.
Bioorganicheskaia khimiia, 20(3), 303-309 (1994-03-01)
Interactions of collagenases I and II (clostridiopeptidases) from Clostridium histolyticum with hexapeptide substrates in which some L-proline residues are replaced by their D-analogues, as well as with the tripeptide chloromethyl ketone Z-Gly-Pro-Gly-CH2Cl were studied. A role of stereochemistry of the
Coşkun Ozcan et al.
Burns : journal of the International Society for Burn Injuries, 28(8), 791-794 (2002-12-05)
Seventy-eight pediatric burn patients treated by enzymatic debridement with collagenase clostridiopeptidase A (CCA), were compared to 41 patients those burn wounds were excised surgically. Patients whose burn wounds were initially assessed as partial-thickness at admission were enrolled in the study.
Dag K Skovseth et al.
Methods in molecular biology (Clifton, N.J.), 360, 253-268 (2006-12-19)
The future ability to manipulate the growth of new blood vessels (angiogenesis) holds great promise for treating ischemic disease and cancer. Several models of human in vivo angiogenesis have been described, but they seem to depend on transgenic support and
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C8176-1G | 04061826682203 |
| C8176-500MG | 04061832700304 |
| C8176-5G | 04061831157635 |
| C8176-25MG | 04061832700298 |
| C8176-100MG | 04061832700281 |