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Protein Loading Buffer for SDS-PAGE- 5X – 1 mL

PROTEIN MAINTENANCE DIET,LOW PROTEIN

PROTEIN MAINTENANCE DIET,LOW PROTEIN

PROTEIN MAINTENANCE DIET,LOW PROTEIN

PROTEIN MAINTENANCE DIET,LOW PROTEIN

PROTEIN MAINTENANCE DIET,LOW PROTEIN

PROTEIN MAINTENANCE DIET,LOW PROTEIN

Component of FastDNA® SPIN Kit for Soil. Used as a stabilization agent during sample lysis of primarily plant tissue. Used in conjunction with a the CLS-VF lysing buffer for homogenization of plant tissue

Component of FastDNA® SPIN Kit for Soil. Used as a stabilization agent during sample lysis of primarily plant tissue. Used in conjunction with a the CLS-VF lysing buffer for homogenization of plant tissue

Protein S

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk’s Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine.

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk’s Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine.

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk’s Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine.

A highly active stable endopeptidase with a broad spectrum of action. Suitable for both protein and nucleic acid isolation

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk’s Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine.

Recombinant Proteinase K is derived from yeast, ≥ 30 U/mg, lyophilized powder.

Recombinant Proteinase K is derived from yeast, ≥ 30 U/mg, lyophilized powder.

Recombinant Proteinase K is derived from yeast, ≥ 30 U/mg, lyophilized powder.

Ready-to-use proteinase K solution, 20 mg/mL in 10 mM Tris-HCl, 1 mM calcium acetate, pH 7.5 containing 50% glycerol.

Ready-to-use proteinase K solution, 20 mg/mL in 10 mM Tris-HCl, 1 mM calcium acetate, pH 7.5 containing 50% glycerol.

Ready-to-use proteinase K solution, 20 mg/mL in 10 mM Tris-HCl, 1 mM calcium acetate, pH 7.5 containing 50% glycerol.

Ready-to-use proteinase K solution, 20 mg/mL in 10 mM Tris-HCl, 1 mM calcium acetate, pH 7.5 containing 50% glycerol.

Proteinase K

Proteinase K

Proteinase K

Proteinase K

Proteinase K

Proteinase K

Proteinase K, Ready-to-use

Proteinase K, Ready-to-use

Recombinant Proteinase K from Tritirachium album expressed in Pichia pastoris.

Prothionamide, NeuroPure

Prothionamide, NeuroPure

PROTHROMBIN

Protocatechuate-3,4-Dioxygenase

Protocatechuate-3,4-Dioxygenase

Protocatechuate-3,4-Dioxygenase

Protocatechuic Acid

Protocatechuic Acid