F3377
N-Formyl-L-methionine
≥90% (TLC)
Synonym(s):
fMet
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About This Item
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product name
N-Formyl-L-methionine, ≥90% (TLC)
Quality Level
Assay
≥90% (TLC)
form
powder
color
white
storage temp.
−20°C
SMILES string
CSCC[C@H](NC=O)C(O)=O
InChI
1S/C6H11NO3S/c1-11-3-2-5(6(9)10)7-4-8/h4-5H,2-3H2,1H3,(H,7,8)(H,9,10)/t5-/m0/s1
InChI key
PYUSHNKNPOHWEZ-YFKPBYRVSA-N
Application
N-Formyl-L-methionine (fMet) is used to identify, differentiate and characterize amino acid N-deformylase(s), N-carbamoylase(s) and N-aminoacylase(s).
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Nature, 452(7183), 108-111 (2008-02-22)
Messenger-RNA-directed protein synthesis is accomplished by the ribosome. In eubacteria, this complex process is initiated by a specialized transfer RNA charged with formylmethionine (tRNA(fMet)). The amino-terminal formylated methionine of all bacterial nascent polypeptides blocks the reactive amino group to prevent
Applied microbiology and biotechnology, 65(6), 686-693 (2004-08-10)
N-carbamoyl-L-cysteine amidohydrolase (NCC amidohydrolase) was purified and characterized from the crude extract of Escherichia coli in which the gene for NCC amidohydrolase of Pseudomonas sp. strain ON-4a was expressed. The enzyme was purified 58-fold to homogeneity with a yield of
Nature structural biology, 9(3), 225-230 (2002-02-06)
The large ribosomal subunit catalyzes peptide bond formation during protein synthesis. Its peptidyl transferase activity has often been studied using a 'fragment assay' that depends on high concentrations of methanol or ethanol. Here we describe a version of this assay
The EMBO journal, 19(19), 5233-5240 (2000-10-03)
The interaction between fMet-tRNA(f)(Met) and Bacillus stearothermophilus translation initiation factor IF2 has been characterized. We demonstrate that essentially all thermodynamic determinants governing the stability and the specificity of this interaction are localized within the acceptor hexanucleotide fMet-3'ACCAAC of the initiator
Journal of immunology (Baltimore, Md. : 1950), 166(2), 1132-1140 (2001-01-06)
H2-M3-restricted presentation of N-formyl methionine (f-Met) peptides to CD8(+) T cells provides a mechanism for selective recognition of bacterial infection. In this report we demonstrate that Listeria monocytogenes infection induces distinct CD8(+) T cell populations specific for each of the
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