recombinant
expressed in E. coli
tag
His tagged
form
liquid
mol wt
27.7 kDa
UniProt accession no.
storage temp.
−70°C
General description
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Application
Biochem/physiol Actions
Physical form
缓冲水溶液包含:40 mM Tris-HCl,pH 8.0,110 mM NaCl、2.2 mM KCl、8 mM 咪唑、0.04% Tween-20 和 20% 甘油
Analysis Note
本产品可以在含有 50 mM HEPES (pH=7.4)、150 mM NaCl、5 mM CaCl2、5 mM (Gly)3、25 mM Abz/Dnp 底物和转肽酶 A 的反应缓冲液 (50 μl) 中 在 30°C 下保温 30 分钟进行分析。 荧光强度在 Ex320nm/Em420nm 处测量。
存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Maximilian W Popp et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(8), 3169-3174 (2011-02-08)
Recombinant protein therapeutics often suffer from short circulating half-life and poor stability, necessitating multiple injections and resulting in limited shelf-life. Conjugation to polyethylene glycol chains (PEG) extends the circulatory half-life of many proteins, but the methods for attachment often lack
Stephan Pritz et al.
The Journal of organic chemistry, 72(10), 3909-3912 (2007-04-17)
Sortase A is a transpeptidase that cleaves at a pentapeptide-motif and subsequently transfers the acyl component to a nucleophile containing N-terminal oligoglycines. We investigate the reaction conditions of the sortase-mediated ligation and demonstrate a useful application by the synthesis of
Peptide-sugar ligation catalyzed by transpeptidase sortase: a facile approach to neoglycoconjugate synthesis.
Sharmishtha Samantaray et al.
Journal of the American Chemical Society, 130(7), 2132-2133 (2008-01-31)
Maximilian W Popp et al.
Nature chemical biology, 3(11), 707-708 (2007-09-25)
Genetically encoded reporter constructs that yield fluorescently labeled fusion proteins are a powerful tool for observing cell biological phenomena, but they have limitations. Sortagging (sortase-mediated transpeptidation) is a versatile chemoenzymatic system for site-specific labeling of proteins with small (<2 kDa)
S K Mazmanian et al.
Science (New York, N.Y.), 285(5428), 760-763 (1999-07-31)
Surface proteins of Gram-positive bacteria are linked to the bacterial cell wall by a mechanism that involves cleavage of a conserved Leu-Pro-X-Thr-Gly (LPXTG) motif and that occurs during assembly of the peptidoglycan cell wall. A Staphylococcus aureus mutant defective in
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