Skip to Content
Merck
All Photos(1)

Key Documents

63187

Sigma-Aldrich

Methoxypolyethylene glycol maleimide

≥90% (NMR), 5,000

Synonym(s):

Polyethylene glycol, MeO-PEG-Mal, PEG-maleimide, mono-Methyl polyethylene glycol 2-maleimidoethyl ether

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
MDL number:
UNSPSC Code:
12162002
PubChem Substance ID:
NACRES:
NA.25

Quality Level

Assay

≥90% (NMR)

mol wt

PEG average Mn 5,000

Ω-end

maleimide

α-end

methoxy

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

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.

related product

Product No.
Description
Pricing

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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
Deanna Davis et al.
Biochimica et biophysica acta. Proteins and proteomics, 1867(4), 382-395 (2019-01-15)
Sphingolipids are diverse lipids with essential, and occasionally opposing, functions in the cell and therefore tight control over biosynthesis is vital. Mechanisms governing this regulation are not understood. Initial steps in sphingolipid biosynthesis take place on the cytosolic face of

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service