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Sigma-Aldrich

Methoxypolyethylenglykol-maleimid

≥90% (NMR), 5,000

Synonym(e):

MeO-PEG-Mal, Monomethyl-polyethylenglykol-2-maleimid-ethylether, PEG-Maleimid

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About This Item

CAS-Nummer:
99126-64-4
MDL-Nummer:
MFCD00803681
UNSPSC-Code:
12162002
PubChem Substanz-ID:
24882458
NACRES:
NA.25

Qualitätsniveau

200

Assay

≥90% (NMR)

Mol-Gew.

PEG average Mn 5,000

Ω-Ende

maleimide

α-Ende

methoxy

Lagertemp.

−20°C

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Anwendung

Methoxypolyethylenglykol-maleimid (MeO-PEG-Mal) wird als Reagenz für die Proteinpegylierung verwendet. Unter PEGylierung wird der Vorgang der kovalenten Bindung von Polyethylenglykol(PEG)-Polymerketten an andere Moleküle, wie Proteine verstanden.

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Preisangaben

06693

Timestrip Plus™ -20 °C

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

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Analysenzertifikate (COA)

Lot/Batch Number
BCCL9369
BCCL4578
BCCJ9516
BCCL0986
BCCH7321

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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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