Biochemistry Unit

Monoclonal & Recombinant Antibodies

We offer a highly customized service, which includes all steps of monoclonal antibody production to satisfy scientific needs as diverse as possible. These range from a general tool working in the most common biochemical techniques (Western, IP, IF, etc.) to more sophisticated ones that fully exploit the power of monoclonal antibodies. Among the latter, we can mention antibodies recognizing post-translational modified epitopes (i.e. phosphorylated, methylated, acetylated epitopes), functional antibodies, inhibitory antibodies, etc. In the last few years, the Mab facility has successfully developed several monoclonal antibody secreting hybridomas against a diverse range of proteins of departmental interest, that are currently in use (see table).

We believe that a powerful reagent that satisfy an experimental need can be generated only through a close interaction between researchers on one side, and the MAb staff on the other, and a merge of reciprocal competencies. We strongly encourage all the researchers interested in monoclonal antibodies to directly partecipate in all the steps of the production, from the definition of the desired product and the antigen selection, to the screening of the hybridomas to isolate a panel of antibodies that covers as many aspects of your research as possible.

Recombinant antibodies

Two recombinant antibody phage display libraries are available at the facility. The panning optimization is still in progress but we already got binders against soluble antigens.

• ScFv format. We use the commercial ETH Gold II library (developed by D. Neri), that is a semi-synthetic library of human origin and a diversity of 3x109.
• Vhh format. We prepared a naïve library starting from the material recovered from 20 llamas and diversity similar to the ETH Gold II.

We expect to be able to offer a regular service with the scFv library in March 2007. In the next future, the Vhh library will remain available only for collaborative projects aimed at its characterization.

IFOM-IEO CAMPUS PUBLICATIONS AND PAPERS CITING mAbs PRODUCED BY THE MAB-SERVICE - download table (.pdf, 64 kb)

ANTIGEN	CLONE(S)	REFERENCES
ABI1	W8-3	Innocenti et al. (2004) Nat Cell Biol, Apr;6(4): 319-27
		Steffen et al. (2004) EMBO J, 23: 749-759
Acetyl-lysine Histone H4	T52.4.1	PATENT NUMBER: WO2004029622
	T25.2.1
CDC20	AR12-4	Sironi et al. (2001) EMBO J, 20(22): 6371-6382
CDC27	SO27	Sironi et al. (2001) EMBO J, 20(22) pp.6371-6382
	ZC51
CDT1	P26A6-1	Melixetian et al. (2004) J Cell Biol 165(4): 473-482
		Ballabeni et al. (2004) EMBO J 23: 3122-3132
EED	AA19-30	Bracken et al. (2003) EMBO J 22(20): 5323-5335
		Pasini et al. (2004) EMBO J 23(20): 4061-4071
		Attwooll et al. (2005) JBC 280(2): 1199-1208
EZH2(N-ter)	AE25-13	Pasini et al. (2004) EMBO J 23(20): 4061-4071
EZH2(middle)	AC22	Attwooll et al. (2005) JBC 280(2): 1199-1208
		Pasini et al. (2004) EMBO J 23(20): 4061-4071
G3BP	A9S4	Soncini et al. (2001) Oncogene Jun 28;20(29):3869-79.
		Rahmouni et al. (2005) Mol Cell Biol. Mar;25(6):2227-41.
MAD1	BB3-8	Steensgaard et al. (2004) EMBO reports 5(6): 626-631
		DeLuca et al. (2003) Current Biology 13: 2103-2109
MAD2	AS55-A12	De Antoni et al. (2005) Current Biology 15: 214-225
p53	AI25-13	Pasini et al. (2004) EMBO J, 23: 4061-4071
ORC2	10E5-1	Ballabeni et al. (2004) EMBO J 23: 3122-3132
p66Shc	BG8	Orsini et al. (2004) JBC 279(24): 25689-25695
RN-tre	15.3	Lanzetti et al. (2004) Nature 429(6989): 309-314
	15.B
SGT1	AN32-1	Steensgaard et al. (2004) EMBO reports 5(6): 626-631
	CI47-A1