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.

CompanyMedChemExpressMedChemExpressMedChemExpressMedChemExpressMedChemExpress
Item[Asp371]-Tyrosinase (369-377), humanAdrenocorticotropic Hormone (ACTH) (1-39), humanAlcohol oxidaseInsulin (swine)L-Lactate dehydrogenase, Microorganism
Catalog NumberHY-P1919HY-P1211HY-P2756HY-P3479HY-P2807
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Quantity1 mg, 5 mg, 10 mg, 25 mg, 50 mg, 100 mg5 mg, 10 mg, 25 mg50 U, 250 U10 mg, 50 mg, 100 mg5 mg, 10 mg, 25 mg
DescriptionTyrosinase 369-377, human is a HLA-A2.1-restricted epitope derived from tyrosinase, has been used to develop tumor-targeted vaccines with mixed efficacy[1][2]Adrenocorticotropic Hormone (ACTH) (1-39), human is a melanocortin receptor agonistAlcohol oxidase is a functional enzyme of methanol utilization pathway and can be isolated from yeast peroxisome[1]Insulin (swine) is a porcine-derived insulin used in diabetes research[1]L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity[1]
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