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L-Lactate Dehydrogenase (L-LDH) 10107085001
Enzyme Commission (EC) Number: 1.1.1.27 ( BRENDA | IUBMB ) General descriptionL-Lactate Dehydrogenase (L-LDH) is an enzyme which is involved in the glycolytic pathway. It is believed to consist of five isotypes, LDH1 to LDH5. It also has a major role in carbohydrate metabolism of human malaria parasites.ApplicationReduction of α-ketoacids to α-hydroxycarboxylic acids or reverse reaction.
It was used in determination of D-Lactate.
Physical form
Suspension in 3.2 M ammonium sulfate solution, pH approximately 6.5Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100, form suspension specific activity ~550 units/mg protein (at 25 °C (1,000 U/mg at 37 °C) with pyruvate as the substrate.) packaging pkg of 10 mL (100 mg) Торговая марка Roche
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L-Malate Dehydrogenase (L-MDH)
Enzyme Commission (EC) Number: 1.1.1.37 ( BRENDA | IUBMB )
Кат. номер 10127256001 10127914001 10127248001 General descriptionL-malate:NAD+ oxidoreductase
The L-malate dehydrogenase enzyme is a nuclear gene product that is synthesized with a 24-residue amino-terminal signal peptide. This peptide is proteolytically cleaved during the translocation of the enzyme to the mitochondrial matrix.ApplicationThe enzyme L-malate dehydrogenase from pig heart has been used to measure PEPCK (phosphoenolpyruvate carboxykinase) activity. The oxaloacetate, produced by PEPCK, is reduced to malate via the oxidation of NADH, which in turn is measured at 340 nm using a spectrophotometer. The enzyme has also been used to measure oxaloacetate by measuring the reduction in NADH spectroscopically at 340 nm.
Biochem/physiol Actions
The enzyme L-malate dehydrogenase from pig heart catalyzes the oxidation of L-malate to oxaloacetate. The enzyme is an NAD-dependent mitochondrial dehydrogenase that functions in the tricarboxylic acid cycle. It is a component of the malate-aspartate shuttle that transports reducing equivalents across the inner mitochondrial membrane in the form of malate.
Quality
Contaminants: <0.002% GOT, <0.01% fumarase and LDH, each luM each, <0.02% HK, <0.002% PGI
Physical form
Suspension in 3.2 M ammonium sulfate solution, pH approximately 6
Solution in 50% glycerol (v/v), pH approximately 7
Preparation Note
Activator: – phosphate
– arsenate
– Mg2+
– Zn2+Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100, form solution, suspension specific activity ~1200 units/mg protein (At 25 °C with oxaloacetate as the substrate.) packaging pkg of 1 mL (10127248001 solution), pkg of 1 mL (10127256001 suspension), pkg of 5 mL (10127914001suspension) Торговая марка Roche optimum pH 7.4-7.5(reduction of oxaloacetate), 9.2-9.5(oxidation of malate) shipped in wet ice storage temp. 2-8°C
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Laminin 11243217001
CAS Number: 114956-81-9 MDL number: MFCD00081739 General descriptionLaminin is purified as laminin-nidogen complex from mouse Engelbreth-Holm-Swarm (EHS) sarcoma. Laminin is a heterotrimer made from , and chain subunits. It is a glycoprotein which is required for the structural scaffolding of basement membranes. Laminin supports growth and differentiation of many cell types including epithelial, endothelial, neural, muscle and liver cells.
Biological activity: Tested for the promotion of adherence of HT-1080 cells.
Species specificity: Active on most mammalian cells.ApplicationLaminin has been demonstrated to promote the attachment and growth of a variety of cells; used for the coating of culture dishes. It has been used for cell adhesion assay. It is recommended for use as a cell culture substratum at 1-2μg/cm2. The optimal concentration does depend on cell type as well as the application or research objectives.
Laminin supports growth and differentiation of many cell types including epithelial, endothelial, neural, muscle and liver cells. It is recommended for use as a cell culture substratum at 1-2 µg/cm2. The optimal concentration does depend on cell type as well as the application or research objectives.
Quality
Purity: 90% (SDS-PAGE) (as laminin nidogen-complex, 1:1)
Sequence
Mouse laminin is composed of three polypeptide chains (A: 400 kD, B1: 230 kD and B2: 220 kD), connected by disulphide bridges, and is glycosylated.
Physical form
Solution, 0.5 mg/ml laminin in 0.15 M NaCl, 2 mM EDTA, 0.05 M Tris-HCl, pH 7.4, sterile
Solution, filtered through 0.2 ?m pore size membrane
Preparation Note
Working concentration: 2 to 5 µg/cm2
2 to 5 µg/cm2 for the coating of cell culture vessels
Storage conditions (working solution): 2 to 8 °C
The undiluted solution is stable at 2 to 8 °C for at least 3 months.
The solution should be thawed carefully at 2 to 8 °C or on ice.Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100 biological source mouse (Engelbreth-Holm-Swarm (EHS) sarcoma) sterility sterile; sterile-filtered assay 90% (SDS-PAGE) form solution mol wt 900 kDa packaging pkg of 1 mg (2 ml) Торговая марка Roche application(s) cell culture | mammalian: suitable UniProt accession no. Q61292, shipped in dry ice storage temp. 20°C Gene Information mouse ... Lamb2(16779)
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Leupeptin
Empirical Formula (Hill Notation): C20H38N6O4 · 0.5H2O4S Linear Formula: C20H38N6O4 · 1/2H2SO4 CAS Number: 103476-89-7 Molecular Weight: 475.59 MDL number: MFCD00037012 PubChem Substance ID: 329817679
Кат. номер 11017101001 11529048001 11034626001 11017128001
Specificity
Leupeptin inhibits serine and thiol proteases such as trypsin, plasmin, proteinase K, kallikrein, papain, thrombin, and cathepsin A and B.
Not affected are -, -, - and - chymotrypsin, pepsin, cathepsin D, elastase, renin, and thermolysin.ApplicationLeupeptin as well as other protease inhibitors like antipain, chymostatin, pepstatin, and phosphoramidon are useful for the protection of proteins during their isolation from tissues or membranes. Leupeptin can be removed from the reaction by dialysis.
Note: To check other protease inhibitors, try our Protease Inhibitor Set including Antipain Dihydrochloride, Aprotinin, Bestatin, Chymostatin, E-64, EDTA-Na2, Leupeptin, Pefabloc SC, Pepstatin, and Phosphoramidon.
Biochem/physiol Actions
Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin. (Loss of cochlear hair cells is believed to be mediated by calpain.)
Features and Benefits
Contents
Synthetic, white powder
Quality
Function test: Performance controlled with trypsin.
Preparation Note
Working concentration: 0.5 to 5 µg/ml (1 to 20 µM)
Comparison of working concentrations of pefabloc with leupeptin and PMSF is in files.
Working solution: Solvent is recommended in distilled water.
Highly soluble in water (1 mg/ml), methanol, ethanol, acetic acid, dimethyl formamide and dimethyl sulfoxide.
Poorly soluble in acetone, chloroform, ethyl ether and n-hexane.
Storage conditions (working solution): -15 to -25 °C
In aqueous solution leupeptin is stable for 1 month at 2 to 8 °C or for at least 6 months at - 15 to -25 °C, stored under nitrogen. For best results, freeze the dissolved inhibitor in aliquots and avoid repeated thawing.
Reconstitution
Highly soluble in water (1 mg/ml). Stable for at least one week at 2 to 8 °C and 6 months frozen in aliquots at -15 to -25 °C.
Analysis Note
Leupeptin gives multiple peaks on HPLC due to equilibria among three forms in solution. Purity determined using three main peaks. Majority of contaminating peptide is racemized leupeptin.Other NotesFor life science research only. Not for use in diagnostic procedures.ПараметрыQuality Level 100, biological source synthetic assay 96.5% form powder mol wt Mr 475.6 packaging pkg of 100 mg (11529048001), pkg of 25 mg (11017128001), pkg of 5 mg (11017101001), pkg of 50 mg (11034626001) Торговая марка Roche solubility H2O: 50 mg/mL shipped in wet ice storage temp. 2-8°C SMILES string OS(O)(=O)=O.CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C=O.CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C=O InChI 1S/2C20H38N6O4.H2O4S/c2*1-12(2)9-16(24-14(5)28)19(30)26-17(10-13(3)4)18(29)25-15(11-27)7-6-8-23-20(21)22;1-5(2,3)4/h2*11-13,15-17H,6-10H2,1-5H3,(H,24,28)(H,25,29)(H,26,30)(H4,21,22,23);(H2,1,2,3,4)/t2*15-,16-,17-;/m00./s1 InChI key CIPMKIHUGVGQTG-VFFZMTJFSA-N
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Liberase™ DH Research Grade
Кат. номер 5401089001 5401054001 General descriptionThe most commonly used method for decellularization procedures, such as tissue dissociation and cell harvesting, is based on the use of proteolytic enzymes. Proteases disrupt the extracellular matrix of tissue to allow the release of individual cells or the harvesting of cultured cells for transfer. The goal of cell isolation is to maximize the yield of dissociated cells that are viable and functionally active.
Liberase enzyme technology comprises methods for purifying clostridial collagenase isoforms to high specific activity, and for blending them together with high-specific-activity neutral protease in optimal ratios for effective dissociation of primary tissues and cultured cells. Liberase DH Research Grade contains highly purified Collagenase I and Collagenase II. These two collagenase isoforms are blended in a precise ratio to each other, and with a high concentration of Dispase®, a non-clostridial neutral protease.
Liberase enzymes are designed to increase the quality and reproducibility of tissue dissociation, and improve the viability and functionality of isolated cells. Liberase Purified Enzyme Blends replace traditional collagenase, which is a crude and variable fermentation by-product of Clostridium histolyticum.ApplicationLiberase™ DH (Dispase High) Research Grade is used for the dissociation of a broad range of tissue types, where high purity of the enzyme blend is necessary for high cell yield and viability. Bacterial by-products, such as endotoxins, are reduced up to several thousand-fold.
It has been used for the digestion of metastatic tumor fragments. It has been used for the enzymatic detachment of human embryonic stem cells colonies.
Features and Benefits- Maximize viability and yield of isolated cells
- Count on higher specific activity of the enzyme blend
- Obtain higher experimental reproducibility
Preparation Note
Stabilizers: Calcium
Working concentration: Liberase Research Grade Enzyme Working Concentration
Liberase enzymes have significantly higher specific activities than traditional collagenases. This means that the working concentration of Liberase Research Grade Purified Enzymes, expressed in mg/ml, will be lower than that of traditional collagenase.
When the application is on the Roche list of applications at www.collagenase.com, use the Liberase Research Grade concentration recommended for that application.
When the application is not included on this list, first use Liberase TM Research Grade at a concentration of 0.08–0.28 Wnsch units/ml.
The goal is to determine the best starting concentration of Liberase Research Grade Enzyme Blends. This is a starting point, and the final concentration may vary due to differences in procedure and lot-to-lot differences in traditional collagenase.
Collagenase Working Concentration
Multiply your previous collagenase working concentration (mg/ml) by its specific activity (Wnsch units/mg, [as determined above]), to obtain Wnsch units/ml. To determine how much Liberase Research Grade Enzyme Blend to use, first multiply your collagenase working concentration (in Wnsch units/ml) times the total volume of your working enzyme solution to obtain the total collagenase activity needed (Wnsch units). Divide the total collagenase activity required by the Liberase Research Grade stock concentration ( “Reconstitution and Storage”). This indicates how many milliliters of Liberase Research Grade Enzyme Blend stock solution to use in your working enzyme solution.
Storage conditions (working solution): Store unused stock solution in single-use aliquots at -15 to -25 °C. Note: Avoid repeated freezing and thawing!
Reconstitution
Reconstitute the lyophilized enzyme with injection-quality sterile water or tissue-dissociation buffer. Do not add serum or other components (e.g., albumin or protease inhibitors) to the dissociation buffer. Enzyme stability is reduced at higher concentrations and warmer temperatures (4 °C). Avoid both the above conditions.
Reconstitute the entire vial. Do not weigh individual aliquots of the lyophilizate. The introduction of moisture into the vial results in a decline in enzymatic activity.
Place vial on ice to rehydrate the lyophilized enzyme.
Gently agitate the vial at 2 to 8 °C until the enzyme is completely dissolved (max. 30 min).
Depending on the type of tissue-dissociation buffer used to dissolve Liberase Research Grade Purified Enzyme Blends, slight precipitations may be observed which readily dissolve in the diluted working solution, and have no influence on enzyme activity.
Remove an aliquot of the stock solution to prepare the working solution.
Reconstitution volume
2 ml (1 vial with 5 mg–10 mg pack size)
10 ml (1 vial with 50 mg–100 mg pack size)
Collagenase Wnsch (units/ml)
13 (1 vial with 5 mg–10 mg pack size)
26 (1 vial with 50 mg–100 mg pack size)
Total Collagenase concentration [mg/ml]
2.5 (1 vial with 5 mg–10 mg pack size)
5.0 (1 vial with 50 mg–100 mg pack size)Other Notes- This product is intended for life science research and in vitro use only. These products are not to be used for diagnostic or clinical applications, such as human islet transplantation.
- All 1st generation Liberase and Liberase Blendzyme products (Liberase HI, CI, RI, PI, Liberase Blendzyme 1, 2, 3, 4) have been replaced by the 2nd generation Liberase Research Grade and Liberase GMP grade enzyme blend portfolios. For instructions concerning the transition from previously used Liberase Enzymes
For life science research only. Not for use in diagnostic procedures.Legal InformationDispase is a registered trademark of Godo Shusei Co., Ltd.
Liberase is a trademark of RocheПараметрыQuality Level 100, form lyophilized packaging pkg of 10 mg (05401054001 [2 x 5 mg]), pkg of 100 mg (05401089001 [2 x 50 mg]) Торговая марка Roche parameter 35-37 °C optimum reaction temp. optimum pH 7.4 shipped in dry ice storage temp. 20°C
Safety InformationRIDADR NONH for all modes of transport Узнать цену -
Liberase™ DL Research Grade
Кат. номер 5466202001 5401160001 General descriptionLiberase™ DH Research Grade contains highly purified Collagenase I and Collagenase II. These two collagenase isoforms are blended in a precise ratio to each other, and with a high concentration of Dispase®, a non-clostridial neutral protease. Liberase™ DL (Dispase Low) Research Grade is used for the dissociation of a broad range of tissue types, where high purity of the enzyme blend is necessary for high cell yield and viability. Bacterial by-products, such as endotoxins, are reduced up to several thousand-fold.ApplicationLiberase® DL (Dispase Low) Research Grade has been used for the isolation of skin stem cells from mice. It is also used for the dissociation of a broad range of tissue types, where high purity of the enzyme blend is necessary for high cell yield and viability. Bacterial by-products, such as endotoxins, are reduced up to several thousand-fold.
Features and Benefits- Maximize viability and yield of isolated cells with an enzyme blend that has less clostripain and trypsin activity, as well as reduced endotoxin content.
- Count on higher specific activity of the enzyme blend as a result of higher Collagenase I + II purity (determined by HPLC analysis).
- Obtain higher experimental reproducibility due to higher lot-to-lot consistency.
Preparation Note
Stabilizers: Calcium
Working concentration: Liberase Research Grade Enzyme Working Concentration
Liberase enzymes have significantly higher specific activities than traditional collagenases. This means that the working concentration of Liberase Research Grade Purified Enzymes, expressed in mg/ml, will be lower than that of traditional collagenase.
When the application is on the Roche list of applications at www.collagenase.com, use the Liberase Research Grade concentration recommended for that application.
When the application is not included on this list, first use Liberase TM Research Grade at a concentration of 0.08–0.28 Wnsch units/ml.
The goal is to determine the best starting concentration of Liberase Research Grade Enzyme Blends. This is a starting point, and the final concentration may vary due to differences in procedure and lot-to-lot differences in traditional collagenase.
Collagenase Working Concentration
Multiply your previous collagenase working concentration (mg/ml) by its specific activity (Wnsch units/mg, [as determined above]), to obtain Wnsch units/ml. To determine how much Liberase Research Grade Enzyme Blend to use, first multiply your collagenase working concentration (in Wnsch units/ml) times the total volume of your working enzyme solution to obtain the total collagenase activity needed (Wnsch units). Divide the total collagenase activity required by the Liberase Research Grade stock concentration ( “Reconstitution and Storage”). This indicates how many milliliters of Liberase Research Grade Enzyme Blend stock solution to use in your working enzyme solution.
Storage conditions (working solution): Store unused stock solution in single-use aliquots at -15 to -25 °C. Note: Avoid repeated freezing and thawing!
Reconstitution
Reconstitute the lyophilized enzyme with injection-quality sterile water or tissue-dissociation buffer. Do not add serum or other components that may influence enzyme activity, such as albumin or protease inhibitors, to the dissociation buffer. Enzyme stability is reduced at higher concentrations and warmer temperatures (4 °C). Avoid both the above conditions.
Reconstitute the entire vial. Do not weigh individual aliquots of the lyophilizate. The introduction of moisture into the vial results in a decline in enzymatic activity.
Place vial on ice to rehydrate the lyophilized enzyme.
Gently agitate the vial at 2 to 8 °C until enzyme is completely dissolved (max. 30 min).
Depending on the type of tissue-dissociation buffer used to dissolve Liberase Research Grade Purified Enzyme Blends, slight precipitations may be observed readily dissolve in the diluted working solution and have no influence on enzyme activity.
Remove an aliquot of the stock solution to prepare the working solution.
Reconstitution volume
2 ml (1 vial with 5 mg–10 mg pack size)
10 ml (1 vial with 50 mg–100 mg pack size)
Collagenase Wnsch (units/ml)
13 (1 vial with 5 mg–10 mg pack size)
26 (1 vial with 50 mg–100 mg pack size)
Total Collagenase concentration [mg/ml]
2.5 (1 vial with 5 mg–10 mg pack size)
5.0 (1 vial with 50 mg–100 mg pack size)Other NotesFor life science research only. Not for use in diagnostic procedures.Legal InformationDispase is a registered trademark of Godo Shusei Co., Ltd.
Liberase is a trademark of Roche
Roche is a registered trademark of Roche Molecular Systems, Inc.ПараметрыQuality Level 100, form lyophilized packaging pkg of 100 mg (05466202001 [2 x 50 mg]), pkg of 10 mg (05401160001 [2 x 5 mg]) Торговая марка Roche parameter 35-37 °C optimum reaction temp. optimum pH 7.4 shipped in dry ice storage temp. 20°C
Safety InformationRIDADR NONH for all modes of transport Узнать цену -
Liberase™ TH Research Grade
Кат. номер 5401151001 5401135001 General descriptionLiberase TH Research Grade contains highly purified Collagenase I and Collagenase II. These two collagenase isoforms are blended in a precise ratio to each other and with a high concentration of Thermolysin, a non-clostridial neutral protease.ApplicationLiberase™ TH (Thermolysin High) Research Grade is used for the dissociation of a broad range of tissue types, where high purity of the enzyme blend is necessary for high cell yield and viability. Bacterial by-products, such as endotoxins, are reduced up to several thousand-fold.
Features and Benefits- Maximize viability and yield of isolated cells
- Count on higher specific activity of the enzyme blend
- Obtain higher experimental reproducibility
- Increase safety
Preparation Note
Stabilizers: Calcium
Working concentration: Liberase Research Grade Enzyme Working Concentration:
Liberase enzymes have significantly higher specific activities than traditional collagenases. This means that the working concentration of Liberase Research Grade Purified Enzymes, expressed in mg/ml, will be lower than that of traditional collagenase.
When the application is on the Roche list of applications at www.collagenase.com, use the Liberase Research Grade concentration recommended for that application.
When the application is not included on this list, first use Liberase TM Research Grade at a concentration of 0.08–0.28 Wnsch units/ml.
The goal is to determine the best starting concentration of Liberase Research Grade Enzyme Blends. This is a starting point, and the final concentration may vary due to differences in procedure and lot-to-lot differences in traditional collagenase.
Collagenase Working Concentration:
Multiply your previous collagenase working concentration (mg/ml) by its specific activity (Wnsch units/mg, [as determined above]), to obtain Wnsch units/ml. To determine how much Liberase Research Grade Enzyme Blend to use, first multiply your collagenase working concentration (in Wnsch units/ml) times the total volume of your working enzyme solution to obtain the total collagenase activity needed (Wnsch units). Divide the total collagenase activity required by the Liberase Research Grade stock concentration ( “Reconstitution and Storage”). This indicates how many milliliters of Liberase Research Grade Enzyme Blend stock solution to use in your working enzyme solution.
Storage conditions (working solution): Store unused stock solution in single-use aliquots at -15 to -25 °C. Note: Avoid repeated freezing and thawing!
Reconstitution
Reconstitute the lyophilized enzyme with injection-quality sterile water or tissue-dissociation buffer. Do not add serum or other components such as albumin or protease inhibitors, to the dissociation buffer. Enzyme stability is reduced at higher concentrations and warmer temperatures (4 °C). Avoid both the above conditions.
Reconstitute the entire vial. Do not weigh individual aliquots of the lyophilizate. The introduction of moisture into the vial results in a decline in enzymatic activity.
Place vial on ice to rehydrate the lyophilized enzyme.
Gently agitate the vial at 2 to 8 °C until enzyme is completely dissolved (max. 30 min).
Depending on the type of tissue-dissociation buffer used to dissolve Liberase Research Grade Purified Enzyme Blends, slight precipitations may be observed which readily dissolve in the diluted working solution and have no influence on enzyme activity.
Remove an aliquot of the stock solution to prepare the working solution.
Reconstitution volume
2 ml (1 vial with 5 mg–10 mg pack size), 10 ml (1 vial with 50 mg–100 mg pack size)
Collagenase Wnsch (units/ml)
13 (1 vial with 5 mg–10 mg pack size), 26 (1 vial with 50 mg–100 mg pack size)
Total Collagenase concentration [mg/ml]
2.5 (1 vial with 5 mg–10 mg pack size), 5.0 (1 vial with 50 mg–100 mg pack size)Other NotesFor life science research only. Not for use in diagnostic procedures.Legal InformationLiberase is a trademark of RocheПараметрыQuality Level 100, form lyophilized packaging pkg of 10 mg (05401135001 [2 x 5 mg]), pkg of 100 mg (05401151001 [2 x 50 mg]) Торговая марка Roche parameter 35-37 °C optimum reaction temp. optimum pH 7.4 shipped in dry ice storage temp. 20°C
Safety InformationRIDADR NONH for all modes of transport Узнать цену -
Liberase™ TL Research Grade 5401020001
General descriptionThe most commonly used method for decellularization procedures, such as tissue dissociation and cell harvesting, is based on the use of proteolytic enzymes. Proteases disrupt the extracellular matrix of tissue to allow the release of individual cells or the harvesting of cultured cells for transfer. The goal of cell isolation is to maximize the yield of dissociated cells that are viable and functionally active.
Liberase Purified Enzyme Blends
Liberase enzymes are blends of highly purified enzymes, designed to increase the quality and reproducibility of tissue dissociation, and improve the viability and functionality of isolated cells. Liberase Purified Enzyme Blends replace traditional collagenase, which is a crude and variable fermentation by-product of Clostridium histolyticum.
Liberase Enzyme Technology
Liberase enzyme technology comprises methods for purifying clostridial collagenase isoforms to high specific activity, and for blending them together with high-specific-activity neutral protease in optimal ratios for effective dissociation of primary tissues and cultured cells.
For additional information, such as manufacturing, technology, or storage, see the Liberase Research Grade Insightsdocument. Further reading on the topic can also be found in the Documents tab.
Roche provides special-quality preparations of Liberase Purified Enzyme Blends, manufactured to meet GMP requirements. For more information on the GMP-grade preparations.
Important Notes:- This product is intended for life science research and in vitro use only. These products are not to be used for diagnostic or clinical applications, such as human islet transplantation.
- All 1st generation Liberase and Liberase Blendzyme products (Liberase HI, CI, RI, PI, Liberase Blendzyme 1, 2, 3, 4) have been replaced by the 2nd generation Liberase Research Grade and Liberase GMP grade enzyme blend portfolios. For instructions concerning the transition from previously used Liberase Enzymes.
ApplicationLiberase™ TL (Thermolysin Low) Research Grade is used for the dissociation of a broad range of tissue types, where high purity of the enzyme blend is necessary for high cell yield and viability. Bacterial by-products, such as endotoxins, are reduced up to several thousand-fold.
This product has been used for the isolation of pancreatic islets from mice.Features and BenefitsLiberase TL Research Grade contains highly purified Collagenase I and Collagenase II. These two collagenase isoforms are blended in a precise ratio to each other and with a low concentration of Thermolysin, a non-clostridial neutral protease.- Maximize viability and yield of isolated cells with an enzyme blend that has less clostripain and trypsin activity, as well as reduced endotoxin content.
- Count on higher specific activity of the enzyme blend as a result of higher Collagenase I + II purit(determined by HPLC analysis)
- Obtain higher experimental reproducibility due to higher lot-to-lot consistency.
- Increase safety with an enzyme that is free of any mammalian or avian tissue-derived raw materials.
Preparation NoteStabilizers: Calcium
Working concentration: Liberase Research Grade Enzyme Working Concentration
Liberase enzymes have significantly higher specific activities than traditional collagenases. This means that the working concentration of Liberase Research Grade Purified Enzymes, expressed in mg/ml, will be lower than that of traditional collagenase.
When the application is on the Roche list of applications at www.collagenase.com, use the Liberase Research Grade concentration recommended for that application.
When the application is not included on this list, first use Liberase TM Research Grade at a concentration of 0.08–0.28 Wnsch units/ml.
The goal is to determine the best starting concentration of Liberase Research Grade Enzyme Blends. This is a starting point, and the final concentration may vary due to differences in procedure and lot-to-lot differences in traditional collagenase.
Collagenase Working Concentration
Multiply your previous collagenase working concentration (mg/ml) by its specific activity (Wnsch units/mg, as determined above), to obtain Wnsch units/ml. To determine how much Liberase Research Grade Enzyme Blend to use, first multiply your collagenase working concentration (in Wnsch units/ml) times the total volume of your working enzyme solution to obtain the total collagenase activity needed (Wnsch units). Divide the total collagenase activity required by the Liberase Research Grade stock concentration ( “Reconstitution and Storage”). This indicates how many milliliters of Liberase Research Grade Enzyme Blend stock solution to use in your working enzyme solution.
Storage conditions (working solution): Store unused stock solution in single-use aliquots at -15 to -25 °C. Note: Avoid repeated freezing and thawing!ReconstitutionReconstitute the lyophilized enzyme with injection-quality sterile water or tissue-dissociation buffer. Do not add serum or other components that may influence enzyme activity, such as albumin or protease inhibitors, to the dissociation buffer. Enzyme stability is reduced at higher concentrations and warmer temperatures (4 °C). Avoid both the above conditions.
Reconstitute the entire vial. Do not weigh individual aliquots of the lyophilizate. The introduction of moisture into the vial results in a decline in enzymatic activity.
Place vial on ice to rehydrate the lyophilized enzyme.
Gently agitate the vial at 2 to 8 °C until enzyme is completely dissolved (max. 30 min).
Depending on the type of tissue-dissociation buffer used to dissolve Liberase Research Grade Purified Enzyme Blends, slight precipitations may be observed which readily dissolve in the diluted working solution and have no influence on enzyme activity.
Remove an aliquot of the stock solution to prepare the working solution
Reconstitution volume
2 ml (1 vial with 5 mg–10 mg pack size), 10 ml (1 vial with 50 mg–100 mg pack size)
Collagenase Wnsch (units/ml)
13 (1 vial with 5 mg–10 mg pack size), 26 (1 vial with 50 mg–100 mg pack size)
Total Collagenase concentration mg/ml
2.5 (1 vial with 5 mg–10 mg pack size), 5.0 (1 vial with 50 mg–100 mg pack size)Storage and StabilityStore at -15–-25 °C. (Store dry. Please note that the expiration date is not printed on the individual vials.)Other NotesFor life science research only. Not for use in diagnostic procedures.Legal InformationLiberase is a trademark of RocheПараметрыQuality Level 100 form lyophilized packaging pkg of 10 mg (2x5 mg) mfr. no. Roche parameter 35-37 °C optimum reaction temp. optimum pH 7.4 shipped in dry ice
Safety Information
