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
ItemAlpha 2 Macroglobulin from human plasma[¹²⁵I]CCL4 (human)PTHrP-(1-21)/PTH-(22-34) (human)TIP39-(9-39) (human/bovine)Trypsin from bovine pancreas(0.22 µm,Filtered)
Catalog NumberNP001158rp175063rp174848rp175305T128775
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Quantity250µg, 1mg5mg, 1mg500µg, 1mg500µg, 1mg50mg
TypeProteinsChelating Agents & LigandsChelating Agents & LigandsChelating Agents & LigandsProteins
DescriptionPurified Native Human Alpha 2 Macroglobulin, Human PlasmaA major serum protein found at concentrations of 240 mg per 100 ml in men and 290 mg per 100 ml in women. Multifunctional, it promotes growth of mammalian cells in culture, stimulates the regeneration of lymphocytes in irradiated mice, ... Read MoreInquireInquireInquireTrypsin 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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