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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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The EMBO journal, 19(9), 2127-2136 (2000-05-03)
Binding of the 50S ribosomal subunit to the 30S initiation complex and the subsequent transition from the initiation to the elongation phase up to the synthesis of the first peptide bond represent crucial steps in the translation pathway. The reactions
Molecular cell, 25(4), 519-529 (2007-02-24)
Translocation requires large-scale movements of ribosome-bound tRNAs. Using tRNAs that are proflavin labeled and single-turnover rapid kinetics assays, we identify one or possibly two kinetically competent intermediates in translocation. EF-G.GTP binding to the pretranslocation (PRE) complex and GTP hydrolysis are
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
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
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
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