Collagenase References

Source:
Clostridium histolyticum
CAS:
9001-12-1
EC:
3.4.24.3
Adams, E. , Antoine, S. and Golstein, A.
Ala-aho, R. and Kahari, V.
An Editorial.
Collagenase and Rheumatoid Arthritis ,
N Engl J Med
279
, 942 , 1968
Ashcroft, S. , Bassett, J. and Randle, P.
Bagchi, N.
What Makes Silica Toxic ,
Br J Industrial Med
49
, 163 , 1992
Barrett, A. , Knight, C. , Brown, M. and Tisljar, U.
Bauer, E. , Eisen, A. and Jeffrey, J.
Bauer, E. , Eisen, A. and Jeffrey, J.
Bauer, E. , Stricklin, G. , Jeffrey, J. and Eisen, A.
Bergmann, U. , Michaelis, J. , Oberhoff, R. , Knauper, V. , Beckmann, R. and Tschesche, H.
Berry, L. and Shuttleworth, C.
Bacterial Collagenase and Collagen Identification ,
Conn Tissue Res
17
, 153 , 1988
Bienkowski, R. , Curran, S. and Berg, R.
Birkedal-Hansen, H.
, Methods Enzymol. Vol. 144 , 140 , 1987
Blanckaert, A. , Mazieres, B. , Eeckhout, Y. and Vaes, G.
Bols, M. , Binderup, L. , Hansen, J. and Rasmussen, P.
Brady, A.
Collagenase in Scleroderma ,
J Clin Invest
56
, 1175 , 1975
Brandhorst, H. , Brandhorst, D. , Hering, B. and Bretzel, R.
Callaway, J. , Garcia, J. , Hersh, C. , Yeh, R. and Gilmore-Hebert, M.
Chesney, C. , Harper, E. and Colman, R.
Human Platelet Collagenase ,
J Clin Invest
53
, 1647 , 1974
Connell, J. and Rousselot, L.
Contractor, H. , Johnson, P. , Chadwick, D. , Robertson, G. and London, N.
Czech, M. and Fain, J.
De Oca, H. and Malinin, T.
De Souza, S. , Pereira, H. , Jacchieri, S. and Brentani, R.
DeBellis, R. , Mandl, I. , MacLennan, J. and Howes, E.
Dono, K. , Gotoh, M. , Fukuzaki, T. , Ohzato, H. , Kanai, T. , Monden, M. and Mori, T.
Donoff, R. , McLenan, J. and Grillo, H.
Dresden, M.
Ducka, P. , Eckhard, U. , Schonauer E. , Kofler, S. , Gottschalk, G. , Brandstetter, H. and Nüss, D.
Eckhard, U. , Schonauer, E. , Ducka, P. , Briza, P. , Nüss, D. and Brandstetter, H.
Eckhard, U. , Schonauer, E. , Nüss, D. and Brandstetter, H.
Eckhard, U. , Schonauer, E. and Brandstetter, H.
Eckhard, U. , Nüss, D. , Ducka P. , Schonauer E. and Brandstetter, H.
Eisen, A. , Bloch, K. and Sakai, T.
Eisen, A. , Jeffrey, J. and Gross, J.
Eisen, A. , Bauer, E. and Jeffrey, J.
Ellis, S. , Nabeshima, K. and Biswas, C.
Emod, I. , Tong, N. and Keil, B.
Evanson, J. , Jeffrey, J. and Krane, S.
Collagenase and Rheumatoid Arthritis ,
N Engl J Med
279
, 942 , 1968
Evanson, J. , Jeffrey, J. and Krane, S.
Ewadh, M. , Tudball, N. and Rose, F.
Ewart, R. , Kornfeld, S. and Kipnis, D.
Fields, G.
Interstitial collagen catabolism. ,
J Biol Chem
288
, 8785-93 , 2013
Foley, J. and Aftonomos, B.
Growth of Human Breast Neoplasms in Cell Culture ,
J Natl Cancer Inst
34
, 217 , 1965
Fox, C. , Stanford, J. and Sampath, A.
Topical Use of Collagenase with Silver Sulfadiazine in Burns , Collagenase , I. Mandl , Gordon and Breach, NY , 145 , 1972
Fujiwara, K. , Sakai, T. , Oda, T. and Igarashi, S.
Gallop, P. , Seifter, S. and Meilman, E.
Gisslow, M. and McBride, B.
Gonzales, T. and Robert-Baudouy, J.
Bacterial Aminopeptidases: Properties and Functions. ,
FEMS Microbiol Rev
18
, 319 , 1996
Gottlieb, A. , Peterkofsky, B. and Udenfriend, S.
Gray, D. , McShane, P. , Grant, A. and Morris, P.
Gross, J. and Lapiere, C.
Gross, J. , Harper, E. , Harris, E. , McCroskery, P. , Highberger. J. , Corbett, C. and Kang, A.
Grubb, J.
Assays for Bacterial Type I Collagenases ,
Meth Enzymol
235
, 594 , 1994
Hamit, H. and Upjohn, H.
Han, H. , Taki, T. , Kondo, H. , Hirono, I. and Aoki, T.
Harper, E. , Bloch, K. and Gross, J.
Harper, E. , Seifter, S. and Hospelhorn, V.
Harper, E.
Harris, E. and Krane, S.
Collagenases ,
N Engl J Med
291
, 557 , 1974
Harris, E. , DiBona, D. and Krane, S.
Collagenases of Human Synovial Fluid ,
J Clin Invest
48
, 2104 , 1969
Harris, E. , Faulkner, C. and Wood, S.
Harris, E. and Farrell, M.
Hausmann, E. and Kaufman, E.
Heindl, M. , Fermandjian, S. and Keil, B.
Hemminki, K.
Hersh, C. , Yeh, R. , Callaway, J. , Garcia, J. and Gilmore-Herbert, M.
Hoover, N. and Ivins, J.
Wound Debridement ,
Arch Surg
79
, 701 , 1959
Houck, J. and Patel, Y.
Collagenolytic Activity of Mammalian Pancreas ,
Proc Soc Exp Biol Med
116
, 382 , 1964
Howard, R. , Christensen, A. , Gibbs, F. and Pesch, L.
Howes, E. , Mandl, I. , Zaffuto, S. and Ackermann, W.
Howes, E.
Howes, E. , MacLennan, J. , Mandl, I. and De Bellis, R.
Huang, C. and Abramson, M.
Jozwiak, J. , Grzela, T. , Jankowska-Steifer, E. , Komar, A. , Moskalewski S. and Martirosian, G.
Lethal Factor of Clostridium histolyticum Kills Cells by Apoptosis. ,
FEMS Immunol Med Microbiol
49
, 296-303 , 2007
Jung, C. , Matsushita, O. , Katayama, S. , Minami, J. , Sakurai, J. and Okabe, A.
Karakiulakis, G. , Papadimitriu, E. , Missirlis, E. and Maragoudakis, M.
Keil, B. , Gilles, A. , Lecroisey, A. , Hurion, N. and Tong, N.
Keller, S. and Mandl, I.
Kerwar, S. , Nolan, J. , Ridge, S. , Oronsky, A. and Slakey, L.
Kin, T. , Johnson, P. , Shapiro, A. and Lakey, J.
Koebe, H. , Muhling, B. , Deglmann, C. and Schildberg, F.
Cryopreserved Porcine Hepatocyte Cultures ,
Chem Biol Interact
121
, 99 , 1999
Kruze, D. and Wojtecka, E.
Lasfargues, E. and Ozzello, L.
Cultivation of Human Breast Carcinomas ,
J Natl Cancer Inst
21
, 1131 , 1958
Lasfargues, E.
Collagenase-Treated Skin Autografts for Rapid Healing of Burns , Collagenase , I. Mandl , Gordon and Breach, NY , 151 , 1972
Lazarus, G. , Brown, R. , Daniels, J. and Fullmer, H.
Human Granulocyte Collagenase ,
Science
159
, 1483 , 1968
Lazarus, G. , Daniels, J. , Brown, R. , Bladen, H. and Fullmer, H.
Lefebvre, V. and Vaes, G.
Lin, M. and Chen, Y.
Liotta, L. , Lanzer, W. and Garbisa, S.
Lwebuga-Mukasa, J. , Harper, E. and Taylor, P.
MacLennan, J. , Mandl, I. and Howes, E.
Bacterial Digestion of Collagen ,
J Clin Invest
32
, 1317 , 1953
Mandl, I.
Collagenases and Elastases , Advances in Enzymology Vol. 23 , F. Nord , Interscience Publ., NY , 163 , 1961
Mandl, I. , Keller, S. and Manahan J.
Mandl, I. , MacLennan, J. , Howes, E. , DeBellis, R. and Sohler, A.
Mandl, I.
Collagenase ,
Science
169
, 1234 , 1970
Matsushita O, Jung CM, Minami J, Katayama S, Nishi N, Okabe A.
Matsushita, O. , Jung, C. , Katayama, S. , Minami, J. , Takahashi, Y. and Okabe, A.
Matsushita, O. , Yoshihara, K. , Katayama, S. , Minami, J. and Okabe, A.
McCroskery, P. , Richards, J. and Harris, E.
McCroskery, P. , Wood, S. and Harris, E.
Merkel, J. , Dreisbach, J. and Ziegler, H.
Collagenolytic Activity of Some Marine Bacteria ,
Appl Microbiol
29
, 145 , 1975
Michaels, S. , Gallop, P. , Seifter, S. and Meilman, E.
Studies on the Specificity of Collagenase ,
Biochim Biophys Acta
29
, 450 , 1958
Mitchell, W.
Miyahara, M. , Hayashi, K. , Berger, J. , Tanzawa, K. , Njieha, F. , Trelstad, R. and Prockop, D.
Moore, S. and Stein, W.
Murphy, G. , McAlpine, C. , Poll, C. and Reynolds, J.
Nagai, N. , Yunoki, S. , Satoh, Y. , Tajima, K. and Munekata, M.
Nagai, Y. , Lapiere, C. and Gross, J.
Nagase, H. , Jackson, R. , Brinckerhoff, C. , Vater, C. and Harris, E.
Nagase, H. , Cawston, T. , DeSilva, M. and Barrett, A.
Nedergaard, J. and Lindberg, O.
The Brown Fat Cell ,
Int Rev Cytol
74
, 187 , 1982
Niedermuller, H. and Petersen, R.
Nixon, J. , Bottomley K. , Broadhurst, M. , Brown, P. , Johnson, W. , Lawton, G. , Marley, J. , Sedgwick, A. and Wilkinson, S.
Noel, J. , Rabinovitch, A. , Olson, L. , Kyriakides, G. , Miller, J. and Mintz, D.
Peck, W. , Birge, S. and Fedak, S.
Pollard, M. and Starr, T.
Robertson, P. , Taylor, R. and Fullmer, H.
Sakamoto, S. , Sakamoto, M. , Goldhaber, P. and Glimcher, M.
Sakamoto, S. , Sakamoto, M. , Goldhaber, P. and Glimcher, M.
Sakamoto, S. , Goldhaber, P. and Glimcher, M.
A New Method for the Assay of Tissue Collagenase ,
Proc Soc Exp Biol Med
139
, 1057 , 1972
Schoellmann, G. and Fisher, E.
A Collagenase From Pseudomonas aeruginosa ,
Biochim Biophys Acta
122
, 557 , 1966
Seifter, S. and Harper, E.
Collagenases , Methods in Enzymology Vol. 19 , G. Perlmann and L. Lorand , Academic Press, NY , 613 , 1970
Seifter, S. and Harper, E.
Collagenases , The Enzymes Vol. 3 , P. Boyer , Academic Press, NY , 649 , 1971
Seifter, S. , Gallop, P. , Klein, L. and Meilman, E.
Seifter, S. , Takahasi, S. and Harper, E.
Seifter, S. and Gallop, P.
, The Proteins, 2nd ed Vol. Vol. IV , H. Neurath , Academic Press, NY , 238 , 1966
Sgaragli, G. , Sen, I. , Baba, A. , Schulz, R. and Cooper, J.
Shibata, A. , Ludvigsen, C. , Naber, S. , McKaneil M. and Lacy, P.
Soberano, M. and Schoellmann, G.
Soberano, M. and Schoellmann, G.
Soru, E. and Zaharia, O.
Sparrow, L. and McQuade, A.
Spina, M. , Garbin, G. , Field, J. and Serafini-Fracassini, A.
Steinbrink, D. , Bond, M. and Van Wart, H.
Steven, F. , Knott, J. , Jackson, D. and Podrazky, V.
Stricklin, G. and Welgus, H.
Sussman, B.
Takahashi, S. and Seifter, S.
Dye-Sensitized Photo-Inactivation of Collagenase A ,
Biochim Biophys Acta
214
, 556 , 1970
Tanaka, T. , Metori, K. , Mineo, S. , Hirotani, M. , Furuya, T. , Matsumoto, H. , Satoh, T. and Kobayashi, S.
Tanzer, M.
Cross-Linking of Collagen ,
Science
180
, 561 , 1973
Taylor, A. , Levy, B. and Simpson, J.
Thompson, M. , Shuplock, N. and Fetterman, S.
Tokoro, Y. , Eisen, A. and Jeffrey, J.
Characterization of a Collagenase from Rat Skin ,
Biochim Biophys Acta
258
, 289 , 1972
Tong, N. , Tsugita, A. and Keil-Dlouha, V.
Toyoshima, T. , Matsushita, O. , Minami, J. , Nishi, N. , Okabe, A. and Itano, T.
Treadwell, B. , Neidel, J. , Pavia, M. , Towle, C. , Trice, M. and Mankin, H.
Treadwell, B. , Towle, C. , Ishizue, K. , Mankin, K. , Pavia, M. , Ollivierre, F. and Gray, D.
Trusler, S.
Vaitkevicius, V. , Simpson, W. and Brennan, M.
Van Wart, H.
Clostridium Collagenases , in Handbook of Proteolytic Enzymes , (Barrett, A., Rawlings, N., and Woessner, J., eds.) , Academic Press, London and San Diego , 416 , 1998
von Hippel, P. , Gallop, P. , Seifter, S. and Cunningham, R.
Vos-Scheperkeuter, G. , Vonk, M. , Wolters, G. and van Schilfgaarde, R.
Wahl, L. , Wahl, S. , Mergenhagen, S. and Martin, G.
Weingarten, H. , Martin, R. and Feder, J.
Welton, R. and Woods, D.
Welton, R. and Woods, D.
Collagenase Production by Achromobacter iophagus ,
Biochim Biophys Acta
384
, 228 , 1975
Woessner, J. and Ryan, J.
Wolters, G. , Vos-Scheperkeuter, G. , van Deijnen, J. and van Schilfgaarde, R.
Woolley, F. , Glanville, R. , Crossley, M. and Evanson, J.
Wuensch, E. and Heidrich, H.
On the Quantitative Determination of Collagenase ,
Hoppe Seylers Z Physiol Chem
333
, 149 , 1963
Wuensch, E. and Heidrich, H.
Yagisawa, S. Morita, F. , Nagai, Y. , Noda, H. and Ogura, Y.
Yiotakis, A. , Hatgiyannacou, A. , Dive, V. and Toma, F.
Yoshida, E. and Noda, H.
Yoshihara, K. , Matsushita, O. , Minami, J. and Okabe, A.
Zimmerman, W.
The Importance of Collagenase for the Local Treatment of Major Burns , Collagenase , I. Mandl , Gordon and Breach, NY , 131 , 1972

Collagenase Products

Description
Activity
Code
Cat. #
Price
Size
Description
Collagenase, Purified
Source:
Clostridium histolyticum
Chromatographically purified. ≤ 50 caseinase units per milligram. Supplied as a lyophilized powder.
Store at 2-8°C.
Activity
≥500 units per mg dry weight
Code
CLSPA
Cat. #
LS005275
Description
Collagenase Vial, NCIS
Source:
Clostridium histolyticum
A component of the NCIS kit. This material is 0.22 micron membrane filtered and lyophilized in autoclaved vials. A vial reconstituted with 5 ml of HBSS or equivalent yields a solution of 300 units/ml of collagenase, Code: CLSPA. Suitable for cell isolation and culture applications.
Store at 2-8°C.
Activity
≥500 units per mg dry weight
Code
CLSPANK
Cat. #
LK003240
Description
Collagenase/Elastase Vial (CLSH)
Source:
Clostridium histolyticum
Enzyme vial of HIS kit that contains 20,000 units of collagenase (Code: CLS-1) and 30 units of elastase (Code: ESL), filtered through 0.22 micron membrane and lyophilized.
Store at 2-8°C.
Activity
≥20,000 units collagense/30 units elastase per vial
Code
CLSH
Cat. #
LK002067
Description
Collagenase, Type 1
Source:
Clostridium histolyticum
The original balance of enzymatic activities. Each lot assayed for collagenase, caseinase, clostripain and tryptic activities. Suggested for epithelial, liver, lung and adrenal primary cell isolations. A dialyzed, lyophilized powder.
Store at 2-8°C.
Activity
≥125 units per mg dry weight
Code
CLS-1
Cat. #
LS004194
Description
Collagenase, Type 2
Source:
Clostridium histolyticum
Prepared to contain higher clostripain activity. Suggested for bone, heart, liver, thyroid and salivary primary cell isolation. Supplied as a dialyzed, lyophilized powder.
Store at 2-8°C.
Activity
≥125 units per mg dry weight
Code
CLS-2
Cat. #
LS004174
Description
Collagenase, Type 3
Source:
Clostridium histolyticum
Lower in secondary proteolytic contaminant activities but with typical collagenase activity. Suggested for mammary primary cell isolation. A dialyzed, lyophilized powder.
Store at 2-8°C.
Activity
≥100 units per mg dry weight
Code
CLS-3
Cat. #
LS004180
Description
Collagenase, Type 4
Source:
Clostridium histolyticum
Prepared to contain lower tryptic activity levels to limit damage to membrane proteins and receptors but with normal to above normal collagenase activity. Suggested for pancreatic islet primary isolation. A dialyzed, lyophilized powder.
Store at 2-8°C.
Activity
≥160 units per mg dry weight
Code
CLS-4
Cat. #
LS004186
Description
Collagenase, Type 5
Source:
Clostridium histolyticum
Partially purified to contain higher collagenase and caseinase activities. A dialyzed, lyophilized powder.
Store at 2-8°C.
Activity
≥450 units per mg dry weight
Code
CLS-5
Cat. #
LS005280
Description
Collagenase, Type 6
Source:
Clostridium histolyticum
Prepared to contain above normal collagenase, FALGPA and Caseinase activities and designed to be enriched with Type II (col H) collagenase.
Store at 2-8°C.
Activity
≥400 units per milligram dry weight
Code
CLS-6
Cat. #
LS005318
Description
Collagenase, Type 7
Source:
Clostridium histolyticum
Prepared to contain 4-5X more collagenase, FALGPA and Caseinase activities than Collagenase 1-4 and with moderate clostripain and tryptic activities.
 
 
Store at 2-8°C.
Activity
≥1,000 units per milligram dry weight
Code
CLS-7
Cat. #
LS005332
Description
Collagenase, Type 1, Filtered
Source:
Clostridium histolyticum
Collagenase, Type 1 (Code: CLS-1), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥125 units per mg dry weight
Code
CLSS-1
Cat. #
LS004214
Description
Collagenase, Type 2, Filtered
Source:
Clostridium histolyticum
Collagenase, Type 2 (Code: CLS-2), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥125 units per mg dry weight
Code
CLSS-2
Cat. #
LS004203
Description
Collagenase, Type 3, Filtered
Source:
Clostridium histolyticum
Collagenase, Type 3 (Code: CLS-3), which is filtered through a 0.22 micron membrane and lyophilized in vials to contain 50 milligrams per vial.
Store at 2-8°C.
Activity
≥100 units per mg dry weight
Code
CLSS-3
Cat. #
LS004206
Description
Collagenase, Type 4, Filtered
Source:
Clostridium histolyticum
Collagenase, Type 4 (Code: CLS-4), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥160 units per mg dry weight
Code
CLSS-4
Cat. #
LS004210
Description
Collagenase, Type 5, Filtered
Source:
Clostridium histolyticum
Collagenase Type 5 (Code: CLS-5), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥450 units per mg dry weight
Code
CLSS-5
Cat. #
LS005286
Description
Collagenase CLSAFA Animal Free/AF
Source:
Clostridium histolyticum
Prepared cultures grown in medium completely devoid of animal based components and designed for bioprocessing applications where introduction of animal derived pathogens must be prevented.
Store at 2-8°C.
Activity
≥150 units per mg dry weight
Code
CLSAFA
Cat. #
LS004152
Description
Collagenase, CLSAFA, Filtered
Source:
Clostridium histolyticum
Collagenase, Animal Free/AF (Code: CLSAFA) which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥150 units per mg dry weight
Code
CLSAFAS
Cat. #
LS004118
Description
Collagenase CLSAFB Animal Free/AF
Source:
Clostridium histolyticum
Prepared from cultures grown in medium completely devoid of animal based components and designed for bioprocessing applications where introduction of animal derived pathogens must be prevented.
Store at 2-8°C.
Activity
≥300 units per mg dry weight
Code
CLSAFB
Cat. #
LS004145
Description
Collagenase, CLSAFB, Filtered
Source:
Clostridium histolyticum
Collagenase, Animal Free/AF (Code: CLSAFB) which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥300 units per mg dry weight
Code
CLSAFBS
Cat. #
LS004124
Description
Collagenase CLSAFC Animal Free/AF
Source:
Clostridium histolyticum
Prepared from cultures grown in medium completely devoid of animal based components and designed for bioprocessing applications where introduction of animal derived pathogens must be prevented.
Store at 2-8°C.
Activity
≥200 units per mg dry weight
Code
CLSAFC
Cat. #
LS004138
Description
Collagenase, CLSAFC, Filtered
Source:
Clostridium histolyticum
Collagenase Animal Free/AF (Code: CLSAFC) which is filtered through a 0.22 micron membrane and lyophilized in vials.
Store at 2-8°C.
Activity
≥200 units per mg dry weight
Code
CLSAFCS
Cat. #
LS004130
Description
Collagenase, Purified, Animal Free
Source:
Clostridium histolyticum
Prepared from cultures grown in medium completely devoid of animal based components and designed for bioprocessing applications where introduction of animal derived pathogens must be prevented.  Chromatographically purified.  ≤ 50 caseinase units per milligram. Supplied as a lyophilized powder.
Store at 2-8°C.
Activity
≥1,500 units per mg dry weight
Code
CLSAFP
Cat. #
LS005294
Description
Collagenase CLSAFD Animal Free/AF
Source:
Clostridium histolyticum
Prepared from cultures grown in medium completely devoid of animal based components and designed for bioprocessing applications where introduction of animal derived pathogens must be prevented.
Store at 2-8°C.
Code
CLSAFD
Cat. #
LS004163
Price
$1,315.00
Description
STEMxyme® 1, Collagenase/Neutral Protease (Dispase)
Source:
Clostridium histolyticum/Bacillus polymyxa
A specialized combination of Animal Free Clostridium histolyticum collagenase (Code: CLSAFB) and animal free Bacillus polymyxa neutral protease with a minimum of 250 CLS units and 1,000 caseinase units per mg dry weight. Designed for stem cell and other primary cell isolations and bioprocessing applications where introduction of potential animal derived pathogens must be prevented.
Store at 2-8°C.
Activity
≥250 CLS/1,000 CAS units per milligram dry weight
Code
STZ1
Cat. #
LS004106
Description
STEMxyme® 2 Collagenase/Neutral Protease (Dispase)
Source:
Clostridium histolyticum/Bacillus polymyxa
A specialized combination of Animal Free Clostridium histolyticum collagenase (Code: CLSAFB) and animal free Bacillus polymyxa neutral protease with a minimum of 250 CLS units and 2,000 caseinase units per mg dry weight. Designed for stem cell and other primary cell isolations and bioprocessing applications where introduction of potential animal derived pathogens must be prevented.
Store at 2-8°C.
Activity
≥250 CLS/2,000 CAS units per milligram dry weight
Code
STZ2
Cat. #
LS004112