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Reference: LS004968
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Apoenzyme. Dried cells grown in B6-deficient media.
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Category: Cell Culture
Reference: LS004970
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Apoenzyme. Dried cells grown in B6-deficient media.
Reference: LS004973
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Apoenzyme. Dried cells grown in B6-deficient media.
Reference: LS005129
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Chromatographically purified. A suspension in 2.6 M ammonium sulfate, pH 8.0.
Reference: LS005130
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Chromatographically purified. A suspension in 2.6 M ammonium sulfate, pH 8.0.
Reference: LS005131
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Chromatographically purified. A suspension in 2.6 M ammonium sulfate, pH 8.0.
Reference: LS005273
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Chromatographically purified. ²50 caseinase units per milligram. Supplied as a lyophilized powder.
Reference: LS005275
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Chromatographically purified. ²50 caseinase units per milligram. Supplied as a lyophilized powder.
Reference: LS005277
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Chromatographically purified. ²50 caseinase units per milligram. Supplied as a lyophilized powder.
Reference: LS005280
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Prepared to contain higher collagenase and caseinase activities. A dialyzed, lyophilized powder.
Reference: LS005282
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Prepared to contain higher collagenase and caseinase activities. A dialyzed, lyophilized powder.
Reference: LS005283
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Prepared to contain higher collagenase and caseinase activities. A dialyzed, lyophilized powder.
Reference: LS005284
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Prepared to contain higher collagenase and caseinase activities. A dialyzed, lyophilized powder.
Reference: LS005286
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Collagenase Type 5 (Code: CLS-5), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Reference: LS005287
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Collagenase Type 5 (Code: CLS-5), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Reference: LS005288
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Collagenase Type 5 (Code: CLS-5), which is filtered through a 0.22 micron membrane and lyophilized in vials.
Reference: LS005290
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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...
Reference: LS005292
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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...
Reference: LS005294
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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...
Reference: LS005301
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Chromatographically purified. A solution in 100 mM sodium chloride. Chymotrypsin and trypsin ² 0.02%.
Reference: LS005302
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Chromatographically purified. A solution in 100 mM sodium chloride. Chymotrypsin and trypsin ² 0.02%.
Reference: LS005304
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Chromatographically purified. A solution in 100 mM sodium chloride. Chymotrypsin and trypsin ² 0.02%.
Reference: LS005305
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Chromatographically purified. A solution in 100 mM sodium chloride. Chymotrypsin and trypsin ² 0.02%.
Reference: LS005318
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Prepared to contain high collagenase activity with a caseinase to collagenase ratio of ~2:1. Designed to be enriched for Type II (col H) collagenase relative to Type I (col G). A dialyzed, lyophilized powder.
Reference: LS005319
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Prepared to contain high collagenase activity with a caseinase to collagenase ratio of ~2:1. Designed to be enriched for Type II (col H) collagenase relative to Type I (col G). A dialyzed, lyophilized powder.
Reference: LS005321
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Prepared to contain high collagenase activity with a caseinase to collagenase ratio of ~2:1. Designed to be enriched for Type II (col H) collagenase relative to Type I (col G). A dialyzed, lyophilized powder.
Reference: LS005323
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Prepared to contain high collagenase activity with a caseinase to collagenase ratio of ~2:1. Designed to be enriched for Type II (col H) collagenase relative to Type I (col G). A dialyzed, lyophilized powder.
Reference: LS005332
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Prepared to contain collagenase and caseinase activities approximately four-fold higher than collagenase Types 1/2. A dialyzed, lyophilized powder.
Reference: LS005333
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Prepared to contain collagenase and caseinase activities approximately four-fold higher than collagenase Types 1/2. A dialyzed, lyophilized powder.
Reference: LS005335
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Prepared to contain collagenase and caseinase activities approximately four-fold higher than collagenase Types 1/2. A dialyzed, lyophilized powder.
Reference: LS005337
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Prepared to contain collagenase and caseinase activities approximately four-fold higher than collagenase Types 1/2. A dialyzed, lyophilized powder.
Reference: LS005410
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Chromatographically purified in a modification of the procedure of Bernardi et al., Biochim. Biophys. Acta, 129, 1 (1966). A dialyzed, lyophilized powder.
Reference: LS005411
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Chromatographically purified in a modification of the procedure of Bernardi et al., Biochim. Biophys. Acta, 129, 1 (1966). A dialyzed, lyophilized powder.
Reference: LS005416
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Chromatographically prepared. A solution in 50% glycerol.
Reference: LS005418
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Chromatographically prepared. A solution in 50% glycerol.
Reference: LS005420
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Chromatographically prepared. A solution in 50% glycerol.
Reference: LS005474
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Chromatographically purified. A dialyzed, lyophilized powder.
Reference: LS005475
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Chromatographically purified. A dialyzed, lyophilized powder.
Reference: LS005477
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Chromatographically purified. A dialyzed, lyophilized powder.
Reference: LS005479
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Chromatographically purified. A dialyzed, lyophilized powder.
Reference: LS005622
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5X crystallized, electrophoretically homogeneous. Supplied as a dialyzed, lyophilized powder. Intrinsic activity ² 0.25 u/mg chymotrypsin.
Reference: LS005623
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5X crystallized, electrophoretically homogeneous. Supplied as a dialyzed, lyophilized powder. Intrinsic activity ² 0.25 u/mg chymotrypsin.
Reference: LS005630
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5X crystallized, electrophoretically homogeneous. Supplied as a dialyzed, lyophilized powder. Intrinsic activity ² 0.25 u/mg chymotrypsin.
Reference: LS005649
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A lyophilized preparation equivalent to Code: RASE. Contains some aggregates as a result of lyophilization but shows no difference in specific activity.
Reference: LS005650
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A lyophilized preparation equivalent to Code: RASE. Contains some aggregates as a result of lyophilization but shows no difference in specific activity.
Reference: LS005655
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A lyophilized preparation equivalent to Code: RASE. Contains some aggregates as a result of lyophilization but shows no difference in specific activity.
Reference: LS005660
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A chromatographically purified, dialyzed, lyophilized powder.
Reference: LS005662
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A chromatographically purified, dialyzed, lyophilized powder.
Reference: LS005677
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Chromatographically purified. Aggregate-free. (Monophoretic on native gel electrophoresis.) A liquid in 100 mM phosphate buffer containing 0.1% v/v phenol as a preservative. Note: The presence of 100 mM phosphate...
Reference: LS005679
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Chromatographically purified. Aggregate-free. (Monophoretic on native gel electrophoresis.) A liquid in 100 mM phosphate buffer containing 0.1% v/v phenol as a preservative. Note: The presence of 100 mM phosphate...
Reference: LS005681
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Chromatographically purified. Aggregate-free. (Monophoretic on native gel electrophoresis.) A liquid in 100 mM phosphate buffer containing 0.1% v/v phenol as a preservative. Note: The presence of 100 mM phosphate...
Reference: LS005710
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A partially purified preparation containing a mixture of RNase A and RNase B. A soluble, dialyzed lyophilized powder.
Reference: LS005715
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A partially purified preparation containing a mixture of RNase A and RNase B. A soluble, dialyzed lyophilized powder.
Reference: LS006122
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Chromatographically purified from Code: BAPC. Ribonuclease ² 0.002% by weight as RNase A using a poly C assay. Phosphodiesterase not detectable when assayed at 0.1 mg/ml with bis(p-nitrophenyl) phosphate. A...
Reference: LS006123
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Chromatographically purified from Code: BAPC. Ribonuclease ² 0.002% by weight as RNase A using a poly C assay. Phosphodiesterase not detectable when assayed at 0.1 mg/ml with bis(p-nitrophenyl) phosphate. A...
Reference: LS006124
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Chromatographically purified from Code: BAPC. Ribonuclease ² 0.002% by weight as RNase A using a poly C assay. Phosphodiesterase not detectable when assayed at 0.1 mg/ml with bis(p-nitrophenyl) phosphate. A...
Reference: LS006130
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Chromatographically purified from Code: BAPC. Ribonuclease ² 0.002% by weight as RNase A using a poly C assay. Phosphodiesterase not detectable when assayed at 0.1 mg/ml with bis(p-nitrophenyl) phosphate. A...
Reference: LS006308
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Chromatographically purified. A lyophilized powder.
Reference: LS006310
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Chromatographically purified. A lyophilized powder.
Reference: LS006311
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Chromatographically purified. A lyophilized powder.
Reference: LS006320
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Chromatographically purified AF bioprocessing grade. Supplied as a lyophilized powder containing glycine as a stabilizer. For the removal of DNA in bioprocessing and primary and stem cell isolation applications. May...
Reference: LS006322
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Chromatographically purified AF bioprocessing grade. Supplied as a lyophilized powder containing glycine as a stabilizer. For the removal of DNA in bioprocessing and primary and stem cell isolation applications. May...
Reference: LS006323
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Chromatographically purified AF bioprocessing grade. Supplied as a lyophilized powder containing glycine as a stabilizer. For the removal of DNA in bioprocessing and primary and stem cell isolation applications. May...
Reference: LS006325
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Chromatographically purified AF bioprocessing grade. Supplied as a lyophilized powder containing glycine as a stabilizer. For the removal of DNA in bioprocessing and primary and stem cell isolation applications. May...
Reference: LS006328
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Chromatographically purified. A lyophilized powder containing glycine as a stabilizer. Contains ² 0.0005% RNase.
Reference: LS006330
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Chromatographically purified. A lyophilized powder containing glycine as a stabilizer. Contains ² 0.0005% RNase.
Reference: LS006331
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Lyophilized in vials containing glycine and calcium as stabilizer.
Reference: LS006332
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Chromatographically purified. A lyophilized powder containing glycine as a stabilizer. Contains ² 0.0005% RNase.
Reference: LS006333
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Lyophilized in vials containing glycine and calcium as stabilizer.
Reference: LS006334
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Lyophilized in vials containing glycine and calcium as stabilizer.
Reference: LS006342
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Supplied as a solution at approximately 2 Kunitz units per microliter (approximately 1 mg/ml) containing 50% glycerol and 1 mM...
Reference: LS006343
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Lyophilized in vials containing glycine and calcium as stabilizer.
Reference: LS006344
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Supplied as a solution at approximately 2 Kunitz units per microliter (approximately 1 mg/ml) containing 50% glycerol and 1 mM...
Reference: LS006348
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Molecular Biology Grade. Chromatographically purified to remove RNase and protease. Supplied as a solution at approximately 2 Kunitz units per microliter (approximately 1 mg/ml) containing 50% glycerol and 1 mM...
Reference: LS006353
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Recombinant protein produced in Pichia pastoris. Free of animal derived components, RNases & proteases. Chromatographically purified. A liquid preparation in 5 mM Calcium Acetate, 4 mg/ml glycine, pH 5.0 and 50%...
Reference: LS006355
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Recombinant protein produced in Pichia pastoris. Free of animal derived components, RNases & proteases. Chromatographically purified. A liquid preparation in 5 mM Calcium Acetate, 4 mg/ml glycine, pH 5.0 and 50%...
Reference: LS006357
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Recombinant protein produced in Pichia pastoris. Free of animal derived components, RNases & proteases. Chromatographically purified. A liquid preparation in 5 mM Calcium Acetate, 4 mg/ml glycine, pH 5.0 and 50%...
Reference: LS006360
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Recombinant protein produced in Pichia pastoris. Free of animal derived components, RNases, and proteases. Chromatographically purified. A lyophilized powder containing glycine as a stabilizer.
Reference: LS006361
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Recombinant protein produced in Pichia pastoris. Free of animal derived components, RNases, and proteases. Chromatographically purified. A lyophilized powder containing glycine as a stabilizer.
Reference: LS006362
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Recombinant protein produced in Pichia pastoris. Free of animal derived components, RNases, and proteases. Chromatographically purified. A lyophilized powder containing glycine as a stabilizer.
Reference: LS006363
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Chromatographically purified. A lyophilized powder.
Reference: LS006365
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Chromatographically purified. A lyophilized powder.
Reference: LS006367
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Chromatographically purified. A lyophilized powder.
Reference: LS006472
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Chromatographically purified. Single basic isozyme with RZ ≥2.9. A lyophilized powder. Suitable for immunoconjugation.
Reference: LS006474
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Chromatographically purified. Single basic isozyme with RZ ≥2.9. A lyophilized powder. Suitable for immunoconjugation.
Reference: LS006476
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Chromatographically purified. Single basic isozyme with RZ ≥2.9. A lyophilized powder. Suitable for immunoconjugation.
Reference: LS008736
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Dried cells. Suitable lysozyme substrate.
Reference: LS008737
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Dried cells. Suitable lysozyme substrate.
Reference: LS008739
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Dried cells. Suitable lysozyme substrate.
Reference: LS009043
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A chromatographically purified, dialyzed, lyophilized powder. Prepared by a modification of the method of Pfrogner, Arch. Biochim. Biophys., 119, 141 (1967).
Reference: LS009044
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A chromatographically purified, dialyzed, lyophilized powder. Prepared by a modification of the method of Pfrogner, Arch. Biochim. Biophys., 119, 141 (1967).
Reference: LS009068
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A highly purified preparation supplied as a lyophilized powder.
Reference: LS009070
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A highly purified preparation supplied as a lyophilized powder.
Reference: LS009071
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A highly purified preparation supplied as a lyophilized powder.
Reference: LS01120
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Prepared by a method developed at Worthington in which native, double-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many DNA binding proteins such as polymerases,...
Reference: LS01122
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Prepared by a method developed at Worthington in which native, double-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many DNA binding proteins such as polymerases,...
Reference: LS01124
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Prepared by a method developed at Worthington in which native, double-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many DNA binding proteins such as polymerases,...
Reference: LS01130
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Prepared by a method developed at Worthington in which denatured, single-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many proteins that are associated with nucleic...
Reference: LS01132
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Prepared by a method developed at Worthington in which denatured, single-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many proteins that are associated with nucleic...
Reference: LS01134
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Prepared by a method developed at Worthington in which denatured, single-stranded calf thymus DNA is covalently bound to cellulose. Suitable for the purification of many proteins that are associated with nucleic...