추천 제품
제품 라인
BioReagent
분석
≥90% (HPLC)
형광
λex 490 nm; λem 518 nm in 0.1 M Tris pH 8.0
적합성
corresponds for coupling to thiols
suitable for fluorescence
저장 온도
2-8°C
SMILES string
Oc1ccc2c(Oc3cc(O)ccc3C24OC(=O)c5cc(ccc45)N6C(=O)C=CC6=O)c1
InChI
1S/C24H13NO7/c26-13-2-5-17-19(10-13)31-20-11-14(27)3-6-18(20)24(17)16-4-1-12(9-15(16)23(30)32-24)25-21(28)7-8-22(25)29/h1-11,26-27H
InChI key
AYDAHOIUHVUJHQ-UHFFFAOYSA-N
유사한 제품을 찾으십니까? 방문 제품 비교 안내
일반 설명
N-(5-Fluoresceinyl) maleimide, also known as fluorescein-5-maleimide (FM), is a fluorescent derivatization reagent. The pH during the derivatization reaction plays a critical role.
애플리케이션
N-(5-Fluoresceinyl) maleimide or fluorescein-5-maleimide is used as a fluorescent biosensor to detect nanoparticles.
N-(5-Fluoresceinyl) maleimide (5-FM) is used to fluorescence label molecules such as proteins and peptides via their thiol groups.
N-(5-Fluoresceinyl) maleimide (5-FM) is used to fluorescence label molecules such as proteins and peptides via their thiol groups.
포장
Bottomless glass bottle. Contents are inside inserted fused cone.
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
Chuck R Smallwood et al.
Molecular microbiology, 72(5), 1171-1180 (2009-05-13)
We studied the reactivity of 35 genetically engineered Cys sulphydryl groups at different locations in Escherichia coli FepA. Modification of surface loop residues by fluorescein maleimide (FM) was strongly temperature-dependent in vivo, whereas reactivity at other sites was much less
Sattasuk Kwanchanok et al.
Bioscience, biotechnology, and biochemistry, 75(10), 2001-2007 (2011-10-08)
Despite recent progress in fluorescence techniques employed to observe protein localization in living cells, the in vitro chloroplastic protein transport assay remains a useful tool for determining the destinations of proteins. Although an in vitro synthesized, radiolabeled precursor protein is
Michael Raba et al.
Journal of molecular biology, 382(4), 884-893 (2008-08-12)
Selected residues of transmembrane domain (TM) IX were previously shown to play key roles in ligand binding and transport in members of the Na(+)/solute symporter family. Using the Na(+)/proline transporter PutP as a model, a complete Cys scanning mutagenesis of
Nicola Giangregorio et al.
Biochimica et biophysica acta, 1767(11), 1331-1339 (2007-10-27)
During substrate translocation mitochondrial carriers cycle between the cytoplasmic-state (c-state) with substrate-binding site open to the intermembrane space and matrix-state (m-state) with the binding site open to the mitochondrial matrix. Here, the accessibility of Cys-58, Cys-136 and Cys-155 of the
Valeria Militello et al.
Biophysical chemistry, 105(1), 133-141 (2003-08-23)
We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The
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