产品名称
N-Formyl-L-methionine, ≥90% (TLC)
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
assay
≥90% (TLC)
form
powder
color
white
storage temp.
−20°C
Quality Level
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.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
J Tomsic et al.
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
Dongli Pan et al.
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
Christine E Carbone et al.
Nature communications, 11(1), 5552-5552 (2020-11-05)
Ribosomes stalled during translation must be rescued to replenish the pool of translation-competent ribosomal subunits. Bacterial alternative rescue factor B (ArfB) releases nascent peptides from ribosomes stalled on mRNAs truncated at the A site, allowing ribosome recycling. Prior structural work
T Chun et al.
The Journal of experimental medicine, 193(10), 1213-1220 (2001-05-23)
Major histocompatibility complex (MHC) class I-restricted CD8(+) T cells play a critical role in the protective immunity against Mycobacterium tuberculosis (Mtb). However, only a few Mtb peptides recognized by MHC class Ia-restricted CD8(+) T cells have been identified. Information on
K Szkaradkiewicz et al.
European journal of biochemistry, 267(13), 4290-4299 (2000-06-24)
Two polypeptides resistant against proteolytic digestion were identified in Thermus thermophilus translation initiation factor 2 (IF2): the central part of the protein (domains II/III), and the C-terminal domain (domain IV). The interaction of intact IF2 and the isolated proteolytic fragments
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