产品编号：15150
产品名称：Pierce Maleimide Activated Plates, 5 Plates
供应商：Pierce
规格：5 PLATES
目录价： 2086
相关信息：
Maleimide Activated Plates, Clear, 8-Well Strip
Formulation: Clear polystyrene 96-well strip plates coated at 100μL/well with proprietary maleimide-presenting molecular solution and blocked at 100μL/well with bovine serum albumin.
Sufficient For: Binding approx. 100 to 150pmol of a sulfhydryl-containing peptide per well
Maleimide Activated Plates
Coat 96-well microplate wells with cysteine-terminated peptides.
Thermo Scientific Pierce Maleimide Activated Plates are ideal for binding sulfhydryl-containing molecules that are difficult to coat onto polystyrene plates, such as peptides that contain a terminal cysteine.
These coated plates are an especially useful tool for assessing specific anti-hapten antibody titers during antibody production. Maleimide Activated Plates are available in clear for colorimetric assays, white for chemiluminescent assays, and black for fluorescent assays.
Highlights:
Pre-blocked to reduce nonspecific binding
Convenient 8-well strip format
Easy (spontaneous) immobilization of peptides derivatized with a terminal cysteine and proteins with free sulfhydryl
Binding Capacity: 100 to 150pmol of a sulfhydryl-containing peptide (307 Da) per well
Activation Level: 100µL
Maleimides react with free sulfhydryl group(s) at pH of 6.5-7.5, forming stable thioether linkages. Reaction with amines becomes significant at pH > 7.5. Some sulfhydryl-containing peptides and proteins may oxidize in solution and form disulfide bonds, which cannot react with maleimides. Disulfide bonds can be reduced to produce free sulfhydryls. The TCEP Disulfide Reducing Gel enables peptide or protein reduction while recovering the sample in the absence of reducing agents. Sulfhydryls can be introduced via amine modification using N-succinimidyl S-acetylthioacetate (SATA) or 2-iminothiolane-HCl (Traut's Reagent).
References:
Ostrowski, M., et al. (2002). J. Virol. 76, 4241-4250.
Nisitani, S., et al. (1999). Proc. Natl. Acad. Sci. USA 96, 2221-2226.
Reinhard, M., et al. (1999). J. Biol. Chem. 274, 13410-13418.