63187
Methoxypolyethylene glycol maleimide
≥90% (NMR), 5,000
Synonyme(s) :
Polyethylene glycol, MeO-PEG-Mal, PEG-maleimide, mono-Methyl polyethylene glycol 2-maleimidoethyl ether
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12162002
ID de substance PubChem :
Nomenclature NACRES :
NA.25
Produits recommandés
Niveau de qualité
Pureté
≥90% (NMR)
Poids mol.
PEG average Mn 5,000
Extrémité Ω
maleimide
Extrémité α
methoxy
Température de stockage
−20°C
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Catégories apparentées
Application
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.
Produit(s) apparenté(s)
Réf. du produit
Description
Tarif
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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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
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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
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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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