4-Methylumbelliferyl-a-L-Iduronide, Cyclohexyl Ammonium Salt

Macerating enzyme from Rhizopus sp. Often used in combination with Cellulase (C32200). Optimum pH range 3.5 - 7.0.

Irreversible serine protease inhibitor of chymotrypsin, kallikrein, papain, subtilisin, thrombin and trypsin. Working Conentration: 0.1-1.0mM.

Purified from chicken egg white, 2x crystallized, dialyzed and supplied as a salt free lyophilized powder. Stable for 3 - 5 years when stored dry at 2°C to 8°C.

From Tritirachium album. Serine protease for protolytic inactivation of nucleases during isolation of DNA and RNA.

RPI offers the highest purity D-Luciferin Potassium Salt for a wide range of bioluminescent applications. Produces bioluminescence when oxidized by firefly luciferase. Allows highly sensitive bioluminescent measurements. Common research uses reporter gene assays, ATP assays, whole animal studies,…

Special savings for ordering X-GAL and IPTG at the same time! Package includes 1 gram bottle of X-Gal and a 1 gram bottle of IPTG.

Reversible inhibitor of cysteine and serine proteases resembling trypsin, Inhibits cathepsin B, kallikrein, papain, plasmin, thrombin and trypsin. Working concentration: 1-10uM

Polyamine growth regulator.

IPTG is combined with X-GAL to detect lac+ colonies or cells in a colorimetric assay. Distinguishes recombinants (white) from non- recombinants (blue) in cloning strategies using vectors such as Lambda-11, M13mp 18 and 19, pUC18 and 19, pUR222 containing the lacZ gene. Dioxane-Free Water…

Chromogenic substrate for B-D-Galactosidase. Produces a deeper blue water insoluble color than X-GAL.

Spectrophotometric substrate for detection of β-D-Glucosidase.

Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein, and plasmin. Material is provided as a solution containing 10,000 KIU/mL of aprotinin.

Fluorescent substrate for β-D-Glucuronidase (GUS) encoded by the gusA gene isolated from E. coli. Fluorescence assay allows quantitation of GUS activity in protein extracts at peak excitation of 365 nm (UV) and a peak emission of 455 nm (blue).

Lyophilized blend of four phosphatase inhibitors for use with animal tissue estracts. Reconstitute with 1ml water to produce a 1 ml concentrate. Contains: Sodium Fluoride Sodium Orthovanadate Sodium Pyrophosphate, decahydrate B-Glycerophosphate Specificity: …

Reversible serine protease inhibitor of a,b,y, and chymostatin, papain, and cathepsins A,B,C. Working concentrations: 10-100uM.

Modification reagent for His and Tyr residues in proteins. Inhibitor of nucleases. DEPC treated water is used in handling of RNA in the laboratory to reduce the risk of RNA being degraded by RNases.

Free PNP: <50ppm

Stable solution of X-GAL and IPTG. Does not contain DMSO or DMF. Solution concentration is 10 mg/ml X-Gal and 8 mg/ml IPTG. Shelf Life: 1 Year

Chromogenic substrate for detection of a-galactosidase activity in yeast Saccharomyces cerevisiae. Used in yeast Two-Hybrid System to detect protein-protein interactions within random libraries. The enzyme a-galactosidase enabels yeast to use disaccharide melibose as a carbon source during growth…

Extracted from yeast. Coenzyme A is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyuvate in the citric acid cycle.

An inhibitor of aspartic proteases. Forms a 1:1 complex with proteases such as pepsin, renin and cathepsin D. Highly selective and does not inhibit thiol proteases, neutral proteases, or serine proteases.

Solution contains 50mg/mL X-GAL in DMF. Protect from light.

Forms a complex with ferrous ions. It can be used as an indicator in oxidation-reduction systems in fitrating ferrous salts. Material passes test for redox indicator and passes test for iron determination.

Spectrophotometric substrate for detection of B-D-Glucuronidase.

Colorimetric and spectrophotometric substrate for detection of β-D-Galactosidase.