Monoclonal Antibodies to Receptors: Probes for Receptor Structure and Function.M. F. GreavesMonoclonal and Anti-Idiotypic Antibodies: Probes for Receptor Structure and Function. Receptor Biochemistry and Methodology, Volume 4.J. Craig Venter , Claire M. Fraser , Jon Lindstrom

1986 ◽  
Vol 61 (1) ◽  
pp. 83-84
Author(s):  
Socrates Tzartos
Keyword(s):  
Monoclonal Antibodies ◽  
Structure And Function ◽  
Craig Venter ◽  
Receptor Structure ◽  
And Function

scholarly journals Monoclonal antibodies reacting with multiple epitopes on the human insulin receptor

1986 ◽  
Vol 235 (1) ◽  
pp. 199-208 ◽  
Author(s):  
M A Soos ◽  
K Siddle ◽  
M D Baron ◽  
J M Heward ◽  
J P Luzio ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Human Placenta ◽  
Structure And Function ◽  
Beta Subunits ◽  
Intact Cells ◽  
Receptor Structure ◽  
Human Insulin Receptor ◽  
And Function

Monoclonal antibodies for the human insulin receptor were produced following immunization of mice with IM-9 lymphocytes and/or purified placental receptor. Four separate fusions yielded 28 antibodies, all of which reacted with receptor from human placenta, liver and IM-9 cells. Some antibodies cross-reacted to varying degrees with receptor from rabbit, cow, pig and sheep, but none reacted with rat receptor. At least 10 distinct epitopes were recognized as indicated by species specificity and binding competition experiments. All of these epitopes appeared to be on extracellular domains of the receptor as shown by binding of antibodies to intact cells. In some cases the epitopes were further localized to alpha or beta subunits by immunoblotting. Several antibodies inhibited binding of 125I-insulin to the receptor, some had no effect on binding, and others enhanced the binding of 125I-insulin. It is concluded that these antibodies will be valuable probes of receptor structure and function.

Monoclonal antibodies to epidermal growth factor receptors in studies of receptor structure and function

1990 ◽  
Vol 3 (3) ◽  
pp. 279-293 ◽  
Author(s):  
Tomoyuki Kawamoto ◽  
Gordon H. Sato ◽  
Kojiro Takahashi ◽  
Mieko Nishi ◽  
Shigehiko Taniguchi ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptors ◽  
Structure And Function ◽  
Epidermal Growth Factor Receptors ◽  
Receptor Structure ◽  
Epidermal Growth ◽  
And Function

scholarly journals Monoclonal Antibodies Generated against Glycoconjugates Recognize Chemical Linkers

Antibodies ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 48
Author(s):  
Jessica Ramadhin ◽  
Vanessa Silva-Moraes ◽  
Thomas Norberg ◽  
Donald Harn
Keyword(s):  
Drug Delivery ◽  
Flow Cytometry ◽  
Monoclonal Antibodies ◽  
Structure And Function ◽  
Enzyme Linked Immunosorbent Assay ◽  
Incomplete Freund’S Adjuvant ◽  
Delivery Platform ◽  
Igg1 Mabs ◽  
Human Milk Oligosaccharide ◽  
And Function

Monoclonal antibodies (mAbs) that recognize glycans are useful tools to assess carbohydrates’ structure and function. We sought to produce IgG mAbs to the human milk oligosaccharide (HMO), lacto-N-fucopentaose III (LNFPIII). LNFPIII contains the Lewisx antigen, which is found on the surface of schistosome parasites. mAbs binding the Lewisx antigen are well-reported in the literature, but mAbs recognizing HMO structures are rare. To generate mAbs, mice were immunized with LNFPIII-DEX (P3DEX) plus CpGs in VacSIM®, a novel vaccine/drug delivery platform. Mice were boosted with LNFPIII-HSA (P3HSA) plus CpGs in Incomplete Freund’s Adjuvant (IFA). Splenocytes from immunized mice were used to generate hybridomas and were screened against LNFPIII conjugates via enzyme-linked immunosorbent assay (ELISA). Three positive hybridomas were expanded, and one hybridoma, producing IgG and IgM antibodies, was cloned via flow cytometry. Clone F1P2H4D8D5 was selected because it produced IgG1 mAbs, but rescreening unexpectedly showed binding to both LNFPIII and lacto-N-neotetraose (LNnT) conjugates. To further assess the specificity of the mAb, we screened it on two glycan microarrays and found no significant binding. This finding suggests that the mAb binds to the acetylphenylenediamine (APD) linker-spacer structure of the conjugate. We present the results herein, suggesting that our new mAb could be a useful probe for conjugates using similar linker spacer structures.

Sign in / Sign up

Export Citation Format

Share Document