Abstract
Rabbit monoclonal antibodies (RmAb) are not routinely obtained by eukaryotic cell fusion techniques. Therefore, we have applied phage display technology to produce a recombinant rabbit Fab molecule directed against the KLH model antigen. The Fab fragments selected from the rabbit phage display library were subcloned in an expression vector to permit the production of a fusion protein comprising a dimer of bacterial alkaline phosphatase (phoA). This fusion protein was directly produced into the periplasmic space of Escherichia coli. We show that a crude extract containing these conjugates can be used in a direct enzyme immunoassay, as exemplified in the case of the KLH antigen.
| Original language | English |
|---|---|
| Pages (from-to) | 201-212 |
| Number of pages | 12 |
| Journal | Journal of Immunological Methods |
| Volume | 213 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jun 1998 |
Fingerprint
Keywords
- Alkaline phosphatase
- Fab fragments
- Phage display
- Rabbit immunoglobulins
- Recombinant antibody
ASJC Scopus subject areas
- Biotechnology
- Immunology
Cite this
Rabbit monoclonal Fab derived from a phage display library. / Foti, Maria; Granucci, Francesca; Ricciardi-Castagnoli, Paola; Spreafico, Adriano; Ackermann, Mathias; Suter, Mark.
In: Journal of Immunological Methods, Vol. 213, No. 2, 06.1998, p. 201-212.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Rabbit monoclonal Fab derived from a phage display library
AU - Foti, Maria
AU - Granucci, Francesca
AU - Ricciardi-Castagnoli, Paola
AU - Spreafico, Adriano
AU - Ackermann, Mathias
AU - Suter, Mark
PY - 1998/6
Y1 - 1998/6
N2 - Rabbit monoclonal antibodies (RmAb) are not routinely obtained by eukaryotic cell fusion techniques. Therefore, we have applied phage display technology to produce a recombinant rabbit Fab molecule directed against the KLH model antigen. The Fab fragments selected from the rabbit phage display library were subcloned in an expression vector to permit the production of a fusion protein comprising a dimer of bacterial alkaline phosphatase (phoA). This fusion protein was directly produced into the periplasmic space of Escherichia coli. We show that a crude extract containing these conjugates can be used in a direct enzyme immunoassay, as exemplified in the case of the KLH antigen.
AB - Rabbit monoclonal antibodies (RmAb) are not routinely obtained by eukaryotic cell fusion techniques. Therefore, we have applied phage display technology to produce a recombinant rabbit Fab molecule directed against the KLH model antigen. The Fab fragments selected from the rabbit phage display library were subcloned in an expression vector to permit the production of a fusion protein comprising a dimer of bacterial alkaline phosphatase (phoA). This fusion protein was directly produced into the periplasmic space of Escherichia coli. We show that a crude extract containing these conjugates can be used in a direct enzyme immunoassay, as exemplified in the case of the KLH antigen.
KW - Alkaline phosphatase
KW - Fab fragments
KW - Phage display
KW - Rabbit immunoglobulins
KW - Recombinant antibody
UR - http://www.scopus.com/inward/record.url?scp=0031825186&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031825186&partnerID=8YFLogxK
U2 - 10.1016/S0022-1759(98)00029-5
DO - 10.1016/S0022-1759(98)00029-5
M3 - Article
C2 - 9692852
AN - SCOPUS:0031825186
VL - 213
SP - 201
EP - 212
JO - Journal of Immunological Methods
JF - Journal of Immunological Methods
SN - 0022-1759
IS - 2
ER -