All Products shortcode with no Uncategorized products. – (SHOP test speed)

Protein A

Protein A

PROTEIN DEPLETION DIET, U.S.P. XV

PROTEIN DEPLETION DIET, U.S.P. XV

PROTEIN DEPLETION DIET, U.S.P. XV

PROTEIN DEPLETION DIET, U.S.P. XV

PROTEIN DEPLETION DIET, U.S.P. XV

PROTEIN DEPLETION DIET, U.S.P. XV

PROTEIN DIET, HIGH

PROTEIN DIET, HIGH

PROTEIN DIET, HIGH

PROTEIN DIET, HIGH

PROTEIN DIET, HIGH

PROTEIN DIET, HIGH

PROTEIN DIET, NORMAL

PROTEIN DIET, NORMAL

PROTEIN DIET, NORMAL

PROTEIN DIET, NORMAL

PROTEIN DIET, NORMAL

PROTEIN DIET, NORMAL

PROTEIN FREE DIET

PROTEIN FREE DIET

PROTEIN FREE DIET

PROTEIN FREE DIET

PROTEIN FREE DIET

PROTEIN FREE DIET

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

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.