Nhs peg nhs

Manufactured by Merck Group

Sourced in United States

NHS-PEG-NHS is a bifunctional crosslinking reagent composed of an N-hydroxysuccinimide (NHS) ester on both ends of a polyethylene glycol (PEG) linker. It is used to covalently link molecules or particles containing primary amine groups.

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Lab products found in correlation

Close spelling variants of this product

Fmoc-NH-(PEG)2-COOH (20 atoms) PEG-NHS Mal-PEG-NHS NHS-PEG-MAL-5000

2 protocols using nhs peg nhs

Synthesis and Characterization of Multifunctional Nanoparticles

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Cadmium oxide, trioctyl phosphine, trioctyl
phosphine oxide, stearic acid, zinc stearate, sulfur powder, selenium
powder, poly(ethylene glycol) methacrylate, N-(3-aminopropyl)-methacrylamide
hydrochloride, 3-sulfopropyl methacrylate, bis[2-(methacryloyloxy)ethyl]phosphate,
ammonium persulfate, NHS-PEG-NHS, 3-amino-3-deoxy-β-cyclodextrin
hydrate (β-CD-NH₂), folic acid, Dulbecco’s
modified Eagle’s medium (DMEM), genistein, amiloride hydrochloride,
MBCD, and sucrose were purchased from Sigma-Aldrich and used as received.
Folate-free RPMI-1640 medium and riboflavin free Ham’s F-12K
medium were purchased from Invitrogen. Hoechst, and lysotracker red
and NBD C6 ceramide green (Golgi tracker green) were purchased from
Life Technology.

Pal S., Dalal C, & Jana N.R. (2017). Supramolecular Host–Guest Chemistry-Based Folate/Riboflavin Functionalization and Cancer Cell Labeling of Nanoparticles. ACS Omega, 2(12), 8948-8958.

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Recombinant Protein Conjugation Protocol

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Recombinant human serum albumin was purchased from InVitria. Mucin from porcine stomach, human transferrin, human hemoglobin, recombinant human insulin, and O,O′-bis[2-(N-succinimidylsuccinylamino)ethyl]polyethylene glycol (NHS-PEG-NHS) with a molecular weight of 2000 Da were purchased from Sigma-Aldrich, USA. O,O′-bis[2-(N-succinimidyl-succinylamino)ethyl]polyethylene glycol (NHS-PEG-NHS) with a molecular weight of 400 Da was purchased from Nanocs Inc., USA.

Habibi N., Mauser A., Raymond J.E, & Lahann J. (2022). Systematic studies into uniform synthetic protein nanoparticles. Beilstein Journal of Nanotechnology, 13, 274-283.

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