Life Science Supplies

Biological supplies and consumables are an essential part of any life science researcher’s toolbox. These supplies, which include nucleic acids, proteins, enzymes and other organic molecules, are used in applications ranging from medical research, drug discovery and diagnostics to agriculture, animal care and forensics. They form the basis of life science and biotechnology experiments that can be used for identification, purification, gene silencing and gene editing. The supplies also serve as standards and reagents in a variety of methods, including western blot, flow cytometry, immunohistochemistry, HPLC, mass spectrometry and more.

Life science supplies may come as standalone items or as part of a kit. The ability to synthesize, engineer and clone these biological and genetic materials has allowed for a wide range of offerings tailored to researchers’ specific needs. Harnessing the natural building blocks of life enables scientists to better understand the inner workings of organisms and work toward the discovery of new drug targets, diagnostic tools, ecological solutions and more.

CompanyAladdin Scientific CorporationAladdin Scientific CorporationAladdin Scientific CorporationAladdin Scientific CorporationAladdin Scientific Corporation
ItemEndoproteinase Lys-C[¹²⁵I]chorionic gonadotropin (human)Recombinant Human EGF ProteinStabilBlock™ Immunoassay StabilizerTrypsin from bovine pancreas(2X,Sterile,Irradiated)
Catalog NumberE382042rp175071rp145392S573239T128772
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Quantity1mg5mg, 1mg100µg, 500µg, 1mg50ml100mg
TypeChelating Agents & LigandsChelating Agents & LigandsProteinsAntibodiesProteins
DescriptionLysyl endopeptidase is an enzyme that hydrolyzes lysyl peptide bonds of nonterminal amino acids. It is highly specific and preferentially cleaves Lys-I-Xaa bonds, including Lys-I-Pro. Used in research as a standard laboratory reagent for enzyme digestion. This is useful to study the primary ... Read MoreInquireInquireProtein:BSA-FreeTrypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa ... Read More
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