dimethyl pimelimidate dihydrochloride

dimethyl pimelimidate dihydrochloride Structure
dimethyl pimelimidate dihydrochloride structure
Common Name dimethyl pimelimidate dihydrochloride
CAS Number 58537-94-3 Molecular Weight 259.17300
Density N/A Boiling Point 301.9ºC at 760mmHg
Molecular Formula C9H20Cl2N2O2 Melting Point ~122 °C (dec.)
MSDS Chinese USA Flash Point 136.4ºC
Symbol GHS07
GHS07
Signal Word Warning

Xenopus HJURP and condensin II are required for CENP-A assembly.

J. Cell Biol. 192(4) , 569-82, (2011)

Centromeric protein A (CENP-A) is the epigenetic mark of centromeres. CENP-A replenishment is necessary in each cell cycle to compensate for the dilution associated to DNA replication, but how this is achieved mechanistically is largely unknown. We have devel...

Cross-linking of the components of lactose synthetase with dimethylpimelimidate.

J. Biol. Chem. 250 , 1434-1444, (1975)

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 inhibi...

Analysis and isolation of human transferrin receptor using the OKT-9 monoclonal antibody covalently crosslinked to magnetic beads.

Anal. Biochem. 199 , 219-222, (1991)

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 cross...

One-step purification of Enterocytozoon bieneusi spores from human stools by immunoaffinity expanded-bed adsorption.

J. Clin. Microbiol. 39 , 1947-1951, (2001)

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 ...

Semisynthetic fluorohydrolases prepared by chemical modification of ribonuclease. David, E., et al.

Enz. Microbiol. Technol. 14 , 885-892, (1992)