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Key Documents

38132

Sigma-Aldrich

N-(5-Fluoresceinyl)maleimide

≥90% (HPLC), BioReagent, suitable for fluorescence

Synonyme(s) :

5-Maleimido-fluorescein

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About This Item

Formule empirique (notation de Hill):
C24H13NO7
Numéro CAS:
Poids moléculaire :
427.36
Numéro MDL:
Code UNSPSC :
12352111
ID de substance PubChem :
Nomenclature NACRES :
NA.32

Gamme de produits

BioReagent

Pureté

≥90% (HPLC)

Fluorescence

λex 490 nm; λem 518 nm in 0.1 M Tris pH 8.0

Adéquation

corresponds for coupling to thiols
suitable for fluorescence

Température de stockage

2-8°C

Chaîne SMILES 

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

Clé InChI

AYDAHOIUHVUJHQ-UHFFFAOYSA-N

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Description générale

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.

Application

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.

Conditionnement

Bottomless glass bottle. Contents are inside inserted fused cone.

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Acute Tox. 4 Oral

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Gloves


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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