38132
N-(5-Fluoresceinyl)maleimide
suitable for fluorescence, ≥90% (HPLC), BioReagent
Sinónimos:
5-Maleimido-fluorescein
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Fórmula empírica (notación de Hill):
C24H13NO7
Número CAS:
Peso molecular:
427.36
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352111
MDL number:
Servicio técnico
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BioReagent
Quality Level
assay
≥90% (HPLC)
fluorescence
λex 490 nm; λem 518 nm in 0.1 M Tris pH 8.0
suitability
corresponds for coupling to thiols, suitable for fluorescence
storage temp.
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
General description
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.
N-(5-Fluoresceinyl) maleimide (5-FM) is used to fluorescence label molecules such as proteins and peptides via their thiol groups.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
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Robert E Dempski et al.
The Journal of biological chemistry, 281(47), 36338-36346 (2006-09-19)
The Na+/K+-ATPase maintains the physiological Na+ and K+ gradients across the plasma membrane in most animal cells. The functional unit of the ion pump is comprised of two mandatory subunits including the alpha-subunit, which mediates ATP hydrolysis and ion translocation
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