Modifying Enzymes
Sigma Aldrich Fine Chemicals Biosciences Apyrase from potatoes, 9000-95-7, MFCD00130542, 500UN
Suitable for manufacturing of diagnostic kits and reagents, ATPase ≥200 units/mg protein. Synonym: Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase, Apyrase from potatoes. Apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. For hydrolysis of organic di and triphosphates, the optimal pH is 6, and for inorganic substrates, the optimal pH is 5.1. Apyrase, from Sigma, has been used in inhibition studies of platelet-aggregation.
Sigma Aldrich Fine Chemicals Biosciences α-Amylase from porcine pancreas | 9000-85-5 | MFCD00081319 | 2.5mu
α-Amylase from porcine pancreas | 9000-85-5 | MFCD00081319 | 2.5mu
Supply Solutions Roche - RNase A, 100 mg; from bovine pancreas; pkg of 100 mg (10109169001) pkg of 25 mg (10109142001)
Roche - RNase A, 100 mg; from bovine pancreas; pkg of 100 mg (10109169001) pkg of 25 mg (10109142001)
Sigma Aldrich Fine Chemicals Biosciences Pepsin, 1g
Pepsin is an aspartic endoproteinase isolated from pig gastric mucosa. It is mainly used for the unspecific hydrolysis of proteins and peptides in acidic media. It also provides a limited hydrolysis of native immunoglobulins to yield biologically active fragments.
Enzo Life Sciences MMP-9 (catalytic domain) (human), (recombinant, E. coli) (10 µg)
Alternative name: Matrix metalloproteinase 9. Gelatinase B. 92 kDa Type IV collagenase. MW: 39 kDa. Purity: ≥95% (SDS-PAGE). Formulation: Liquid. In 50mM TRIS, pH 7.5, containing 1mM calcium chloride, 300mM sodium chloride, 5μM zinc chloride, 0.1% Brij-35 and 15% glycerol. Source: Produced in E. coli. Active recombinant matrix metalloproteinase-9 (MMP-9, gelatinase B, 92 kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Phe107-Pro449 (NM_004994), which comprises the catalytic/fibronectin domain of human MMP-9, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-9 which lacks the C-terminal hemopexin domain. Activity toward its targets, such as gelatin. CASein, or peptide substrates, is unaffected. UniProt: P14780. Handling: Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. Long Term Storage: -80°C
Supply Solutions Roche - Proteinase K,Recomb.,Pcr Grd.Lyo,2X250Mg
Roche - Proteinase K,recomb.,PCR Grd.lyo,2x250mg; Lyophilized from Pichia pastoris; pkg of 100 mg (03115879001) pkg of 25 mg (03115836001) pkg of 2 x 250 mg (03115801001) pkg of 4 x 250 mg (0311582001)
New England Biolabs, Inc. Exonuclease VII – 200 units
Exonuclease VII, (Exo VII) derived from E. coli, cleaves single-stranded DNA (ssDNA) from both 5' to 3' and 3' to 5' direction. This enzyme is not active on linear or circular dsDNA. It is useful for removal of single stranded oligonucleotide primers from a completed PCR reaction when different primers are required for subsequent PCR reactions. Digestion of ssDNA by Exonuclease VII is metal-independent.
Supply Solutions Roche - Proteinase K,Recomb.,Pcr Grd.Lyo.,100 Mg
Roche - Proteinase K,recomb.,PCR Grd.lyo.,100 mg; Lyophilized from Pichia pastoris; pkg of 100 mg (03115879001) pkg of 25 mg (03115836001) pkg of 2 x 250 mg (03115801001) pkg of 4 x 250 mg (0311582001)
Supply Solutions Roche - b-Glucuronidase/Arylsulfatase; from Helix pomatia; pkg of 10 mL (10127698001) pkg of 2 mL (10127060001)
Roche - b-Glucuronidase/Arylsulfatase; from Helix pomatia; pkg of 10 mL (10127698001) pkg of 2 mL (10127060001)
Supply Solutions Roche - Proteinase K,Recomb.,Pcr Grd. Lyo.,25 Mg
Roche - Proteinase K,recomb.,PCR Grd. lyo.,25 mg; Lyophilized from Pichia pastoris; pkg of 100 mg (03115879001) pkg of 25 mg (03115836001) pkg of 2 x 250 mg (03115801001) pkg of 4 x 250 mg (0311582001)
Sigma Aldrich Fine Chemicals Biosciences Neuraminidase (Sialidase) from Vibrio cholerae
Neuraminidase is an acylneuraminyl hydrolase which hydrolyzes terminal N- or O-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate: α2,6 > α2,3 > α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids. Noteworthy, for the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials.
Sigma Aldrich Fine Chemicals Biosciences Phosphatase, Acid from sweet potato ammonium sulfate suspension, ≥10.0 units/mg protein (modified Warburg-Christian) | 9001-77-8 | MFCD00131847 | 500un
Phosphatase, Acid from sweet potato ammonium sulfate suspension, ≥10.0 units/mg protein (modified Warburg-Christian) | 9001-77-8 | MFCD00131847 | 500un
Sigma Aldrich Fine Chemicals Biosciences Lipase from porcine pancreas | 9001-62-1 | MFCD00131509 | 100g
Lipase from porcine pancreas | 9001-62-1 | MFCD00131509 | 100g
Sigma Aldrich Fine Chemicals Biosciences Phosphatase, Alkaline from bovine intestinal mucosa buffered aqueous solution, >=2,000 DEA units/mg protein | 9001-78-9 | MFCD00131849 | 2KU
Phosphatase, Alkaline from bovine intestinal mucosa buffered aqueous solution, >=2,000 DEA units/mg protein | 9001-78-9 | MFCD00131849 | 2KU
Sigma Aldrich Fine Chemicals Biosciences Thrombin from human plasma lyophilized powder, >=2800 NIH units/mg protein (E1%/280, 18.3) | 9002-04-4 | MFCD00082072 | 250UN
Thrombin from human plasma lyophilized powder, >=2800 NIH units/mg protein (E1%/280, 18.3) | 9002-04-4 | MFCD00082072 | 250UN