Recombinant human Asf1α

 

Catalog # : EPX-004-REP

 

Source : Human

 

Expressed in : E. coli

 

Quantity : 25 g of recombinant Asf1a at 0,5g /l

 

 

 

 

Protein details:

 

Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (1). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (2, 3). Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4. Recombinant Asf1a was produced in E. coli as a N-terminal GST fusion, purified using FPLC and formulated in a storage buffer containing 20 mM Tris pH 7.65, 150 mM NaCl, 1 mM DTT, 10% glycerol. Protein concentration was determined by spectrometry. >95% purity by SDS-PAGE.

 

 

Quality control:

 Each lot has been evaluated by 12% Tris Glycine SDS-PAGE.


 

center
SDS-PAGE gel of recombinant human Gst-Asf1a (Lane 2).  Lane 1, protein molecular weight marker.

 

 

 

Storage:

 

-80C

 

 

Guarantee:

 

For research use only. Products guaranteed stable for 2 years from date of receipt when stored properly.

 

 

Purity:

 

>98% purity by SDS PAGE.

 



References:

1- Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.A human homologue of yeast anti-silencing factor has histone chaperone activity.
Genes Cells 5:221-233(2000).
2- Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R., Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C., Ochsenbein F. Structural basis for the interaction of Asf1 with histone H3 and its functional implications. Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005).
3- Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.
Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A., Dunbrack R., Adams P.D., Marmorstein R. Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Nat. Struct. Mol. Biol. 13:921-929(2006).


 

 

 


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