63187
Methoxypolyethylene glycol maleimide
≥90% (NMR), 5,000
Sinônimo(s):
Polyethylene glycol, MeO-PEG-Mal, PEG-maleimide, mono-Methyl polyethylene glycol 2-maleimidoethyl ether
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About This Item
Número CAS:
Número MDL:
Código UNSPSC:
12162002
ID de substância PubChem:
NACRES:
NA.25
Produtos recomendados
Nível de qualidade
Ensaio
≥90% (NMR)
peso molecular
PEG average Mn 5,000
Ω-final
maleimide
α-final
methoxy
temperatura de armazenamento
−20°C
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Categorias relacionadas
Aplicação
Methoxypolyethylene glycol maleimide (MeO-PEG-Mal) is used as a protein pegylation reagent. PEGylation is the process of covalently attaching polyethylene glycol (PEG) polymer chains to other molecule such as proteins.
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Nº do produto
Descrição
Preços
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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K Ananda et al.
Analytical biochemistry, 374(2), 231-242 (2007-12-27)
The design of the extension arm-facilitated PEGylation (EAFP) of proteins takes advantage of the high selective and quantitative aspects of the thiol-maleimide reaction. However, the efficiency of EAFP with hemoglobin varied with the batches of maleimide-PEG. The low level of
R J Goodson et al.
Bio/technology (Nature Publishing Company), 8(4), 343-346 (1990-04-01)
We have modified recombinant interleukin-2 (rIL-2) to facilitate site-directed covalent attachment of monomethoxy polyethylene glycol (PEG). The site chosen for modification and subsequent covalent attachment with PEG (PEGylation) was the single glycosylation position found in the native interleukin-2 (IL-2). The
Jiankun Qie et al.
Drug metabolism letters, 1(3), 232-240 (2007-08-01)
Site-specific mono-PEGylations were performed in different conformational regions of Thymosin alpha 1 (T alpha 1) by introducing one cysteine residue into the chosen site and coupling with thiol-specific mPEG-MAL reagent. Results demonstrated that PEGylated sites and regions influenced the conformations
Lidia Wrobel et al.
Scientific reports, 6, 27484-27484 (2016-06-07)
Disulfide bond formation is crucial for the biogenesis and structure of many proteins that are localized in the intermembrane space of mitochondria. The importance of disulfide bond formation within mitochondrial proteins was extended beyond soluble intermembrane space proteins. Tim22, a
Leah C Ray et al.
Nature chemical biology, 14(6), 538-541 (2018-05-18)
Polyprenol phosphate phosphoglycosyl transferases (PGTs) catalyze the first membrane-committed step in assembly of essential glycoconjugates. Currently there is no structure-function information to describe how monotopic PGTs coordinate the reaction between membrane-embedded and soluble substrates. We describe the structure and mode
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