Bioreagents

Protease Inhibitor Cocktail VII, DMSO-Free for His Tag Seque

Protease Inhibitor Cocktail VII, for His Tag Sequences

Protease V.8 specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. In the presence of ammonium, the specificity is limited to glutamic sites.

Protein A

Protein A

Protein A

Recombinant protein A binds immunoglobulins (primarily IgG) at the Fc region with high affinity. In some cases, IgM and IgA will also bind. This property provides a rapid, simple and economical method for purification and analysis of a broad-spectrum of antibodies. Fractionation of IgG subclasses can also be performed using recombinant protein A. Because of its high affinity for immunoglobulins of many species and its low level of non-specific binding, recombinant protein A is useful for the study of cell surface antigens and receptors, and for detecting antibody-secreting cells. Recombinant protein A is produced in an E. coli strain which contains the gene for mature protein A from Staphylococcus aureus Cowan I strain.

Protein A

Protein A

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 G is a monomeric protein lacking cysteine residues. Recombinant Protein G is a highly stable surface receptor that is capable of binding the Fc portion of immunoglobulins, especially IgGs from a large number of species. Preparation:Protein G is from Streptococcus sp.expressed in E. coli.

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

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.