Pepsin 1: 3000 (porcine source) is an endopeptidase that breaks down proteins into smaller peptides. Pepsin is applied in the hydrolysis of proteins. Pepsin 1: 3000 serves in protein proteolysis to cleave aromatic amino acids like phenylalanine and tyrosine from the N-terminus of proteins. …

Molecular Biology Grade Specific activity (25° C): ≥95U/mg Solubility (1%, water): Clear and haze-free Glucose Oxidase: Catalase ratio >100:1 Unit Definition: The amount of enzyme which causes the oxidation of 1 micromole of glucose per minute at 25 C, pH 7.0 50 ku

1,000 U Conjugation Grade Ammonium Sulfate Suspension Source: Calf Intestine Adenosine Deaminase: <=0.001% Concentration (37 C): >7500U/ml Phosphodiesterase: <=0.001% DNase, RNase, and Protease: None Specific activity (37 C, pH 10.5, DEA): >1500U/mg

Protease which cleaves specifically at the -COOH side of arginie and lysine. TPCK-treated Trypsin is a serine endopeptidate Trypsin is treated with TPCK to inactivate any remaining chymotryptic activity This type of trypsin is modified by acetyltion of the sigma-amino groups of lysine…

Yeast lytic enzyme

The bioWORLD bioPlus™ 1:300 trypsin is mainly used in cell culture experiments. When combined with other enzymes, it is used to reduce inflammation and swelling.

A serine proteinase used to inactivate RNAse and DNAse in RNA and DNA isolation protocols. Useful in the study of membrane and protein structure. Proteinase K is a highly active protease (MW 28,500 Da) isolated from the fungus Tritirachium album . The enzyme exhibits broad specificity on…

From Trichadema Viride. Enzyme mixture often used in combination with Macerozyme R-10 (M22010) for isolation of plant protoplasts. One unit of Cellulase will liberate 1.0 µmole of glucose from carboxymethyl cellulose. Lyophilized powder Optimum pH range: 4-5

Enzyme used in purification protocols of genomic and plasmid DNA to lyse bacterial cells.

Also known as Poly-(1,4-a-D-galacturonide)glycanohydrolase. Used in plant protoplast preparation to digest cell wall prior to organelle isolation.

The bioWORLD bioPLUS™ trypsin 1:250 is suitable for laboratory and biological research use. Application: For Research & Laboratory Use Only, For in Vitro Lab Use Only. Not For Human Use or Consumption

A serine peptidase that cleaves at internal peptide bonds on the carboxyl-side of arginine and lysine residues. USP Grade Activity (min.) at 25 C >2,500U/mg Chymotrypsin 5.0% Unit Definition: The amount of enzyme which causes an increase in absorbance of 0.003 per minute at 25 C…

Enzyme found in lac+ bacterial cells that catalyzes the cleavage of -linked terminal galactose-containing substrates. Lyophilized powder Source: E. coli Conjugation grade Activity (37°C):800-1000U/mg protein Unit definition: One unit will hydrolyze 1.0 μmole of…

Enables antibody or protein labeling with alkaline phosphatase (AP) in less than 3 hours, saving you several hours over standard maleimide/thiol methods. AP is supplied ready-to-use, preactivated and requires no activation or purifi cation. Suffi cient reagents are provided to conjugate 3 samples,…

Isolated from Chick Pea Supplied as lyophilized powder

The bioWORLD bioPLUS™ peroxidase (horseradish) (HRP) is suitable for research and laboratory use. Application: Used As An Indicator Enzyme Conjugated To Proteins Such As Antibodies

DNase I is an endonuclease derived from bovine pancreas that will degrade double-stranded DNA in the presence of divalent cations, producing 3'-OH oligonucleotides. Mg+2 in the reaction solution causes the enzyme to produce nicks in double-stranded DNA, while in the presence on Mn+2, DNase I…

Lectin isolated from Triticum vulgaris (wheat germ). Wheat germ agglutinin (WGA) is used for binding to variety of receptors, agglutination reaction and used as ligand for purification of specific membrane proteins.

Malate Dehydrogenase, Ammonium Sulfate Suspension

The S1 Nuclease degrades single-stranded nucleic acids, releasing 5'-phosphoryl mono- or oligonucleotides. It is more active on DNA than on RNA. The S1 Nuclease exhibits 3'-phosphomonoesterase activity. The enzyme is a glycoprotein with MW of 29 kD monomer. Source Aspergillus oryzae

Lectin isolated from Erythrina cristagalli (coral tree) seeds. Agglutination activity is expressed in mg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, of a 1 µg per mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of…