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일반 설명
Dimethyl pimelimidate dihydrochloride is a homobifunctional cross-linking reagent used in crosslinking, protein interaction and protein modification. It typically reacts with primary amines in the pH range 7.0-10.0 to form amidine bonds.
애플리케이션
Dimethyl pimelimidate dihydrochloride has been used to develop a technique for isolating Enterocytozoon bieneusi spores directly from human stool samples with a high degree of purity, which opens up new approaches for studying this parasite.
주의사항
The reagent is readily hydrolyzed at neutral pH.
기타 정보
Note that the amidine linkage preserves original primary amine positive charge. Incorporates a seven atom linker.
신호어
Warning
유해 및 위험 성명서
Hazard Classifications
Skin Irrit. 2
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
dust mask type N95 (US), Eyeshields, Gloves
이미 열람한 고객
G B Karlsson et al.
Analytical biochemistry, 199(2), 219-222 (1991-12-01)
A method is described for the use of magnetic beads as a solid phase for the immunoprecipitation of labeled proteins. The anti-human transferrin receptor monoclonal antibody OKT-9 has been coupled to sheep anti-mouse IgG1-coated magnetic beads using the crosslinking agent
I Accoceberry et al.
Journal of clinical microbiology, 39(5), 1947-1951 (2001-04-28)
An original, reliable, and reproducible method for the purification of Enterocytozoon bieneusi spores from human stools is described. We recently reported the production of a species-specific monoclonal antibody (MAb) 6E52D9 immunoglobulin G2a (IgG2a) raised against the exospore of E. bieneusi
K Brew et al.
The Journal of biological chemistry, 250(4), 1434-1444 (1975-02-25)
The cross-linking of the two components of lactose synthetase, alpha-lactalbumin and a galactosyltransferase, with dimethylpimelimidate was examined. The extent of the cross-linking at pH 8.1 was found to be dependent upon the presence of substrates or inhibitors for the galactosyltransferase.
Semisynthetic fluorohydrolases prepared by chemical modification of ribonuclease.
David, E., et al.
Enz. Microbiol. Technol., 14, 885-892 (1992)
Kevin Michael Boehm et al.
BMC bioinformatics, 20(1), 7-7 (2019-01-07)
To further our understanding of immunopeptidomics, improved tools are needed to identify peptides presented by major histocompatibility complex class I (MHC-I). Many existing tools are limited by their reliance upon chemical affinity data, which is less biologically relevant than sampling
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