نتایج جستجو برای: camel heavy chain antibody

تعداد نتایج: 564005  

2009
L Gautam S C Mehta R S Gahlot K Gautam

Six New World Camelidae microsatellite primer pairs were used to investigate the genetic polymorphism in Jaisalmeri camel. Polymerase chain reactions were carried out for 30 unrelated camels of Jaisalmeri breed. The amplification products were resolved in 6% (denaturing) urea PAGE and stained with silver nitrate. All the 6 microsatellite primer pairs were found polymorphic in Jaisalmeri camel. ...

Journal: :Blood 1992
K S Landreth R Narayanan K Dorshkind

Progression of B-lymphocyte development in the bone marrow of postnatal mammals is marked by progressive rearrangement and expression of immunoglobulin (Ig) heavy- and light-chain genes. Following productive VHDJH gene rearrangement in the Ig heavy-chain gene complex, mu-heavy chain is the first Ig gene product expressed in cells committed to the B-lymphoid differentiation pathway. Interleukin ...

Journal: :The Journal of biological chemistry 1993
J Ping J F Schildbach S Y Shaw T Quertermous J Novotny R Bruccoleri M N Margolies

In certain instances, antibody variable region mutations outside of the antigen-combining site influence antigen binding. We reported previously that a heavy chain mutation (Ser-94-->Arg) decreased binding of the anti-digoxin antibody 40-150, whereas an additional signal peptide mutation at the -2 position (Gln-->Pro) causing NH2-terminal 2-residue truncation partially restored binding. To asse...

2012
Wei-Gang Hu Junfei Yin Damon Chau Laurel M. Negrych John W. Cherwonogrodzky

Ricin is regarded as a high terrorist risk for the public due to its high toxicity and ease of production. Currently, there is no therapeutic or vaccine available against ricin. D9, a murine monoclonal antibody developed previously in our laboratory, can strongly neutralize ricin and is therefore a good candidate for humanization. Humanization of D9 variable regions was achieved by a complement...

Journal: :Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 2014
Yuki Yagi Kazuaki Kakehi Takao Hayakawa Shigeo Suzuki

We evaluated the performance of a commercial microchip electrophoresis instrument (LabChip(®) GXII) for the evaluation of change of degradation species of therapeutic antibodies in stability testing. This system requires a sample volume of only 5 μg, and indicates fine resolution of size variant species such as light chain, heavy chain, non-glycosylated heavy chain and various degradation speci...

Journal: :Blood 1988
R A De La Cadena F A Baglia C A Johnson R E Wenk R Amernick P N Walsh R W Colman

We have isolated and probed the mechanism of action of two naturally occurring antibodies (Baltimore and Winston-Salem) against factor XI (FXI), that developed in patients congenitally deficient in FXI after replacement therapy. Purification on immobilized protein A and neutralization with monospecific antibodies against IgG heavy and light chain subtypes indicated that both antibodies were of ...

Journal: :Science 2009
Joshua A Weinstein Ning Jiang Richard A White Daniel S Fisher Stephen R Quake

Despite tremendous progress in understanding the nature of the immune system, the full diversity of an organism's antibody repertoire is unknown. We used high-throughput sequencing of the variable domain of the antibody heavy chain from 14 zebrafish to analyze VDJ usage and antibody sequence. Zebrafish were found to use between 50 and 86% of all possible VDJ combinations and shared a similar fr...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2013
Jiang Zhu Gilad Ofek Yongping Yang Baoshan Zhang Mark K Louder Gabriel Lu Krisha McKee Marie Pancera Jeff Skinner Zhenhai Zhang Robert Parks Joshua Eudailey Krissey E Lloyd Julie Blinn S Munir Alam Barton F Haynes Melissa Simek Dennis R Burton Wayne C Koff James C Mullikin John R Mascola Lawrence Shapiro Peter D Kwong

Next-generation sequencing of antibody transcripts from HIV-1-infected individuals with broadly neutralizing antibodies could provide an efficient means for identifying somatic variants and characterizing their lineages. Here, we used 454 pyrosequencing and identity/divergence grid sampling to analyze heavy- and light-chain sequences from donor N152, the source of the broadly neutralizing antib...

Journal: :Journal of virology 2017
Wanbo Tai Yufei Wang Craig A Fett Guangyu Zhao Fang Li Stanley Perlman Shibo Jiang Yusen Zhou Lanying Du

Middle East respiratory syndrome coronavirus (MERS-CoV) binds to cellular receptor dipeptidyl peptidase 4 (DPP4) via the spike (S) protein receptor-binding domain (RBD). The RBD contains critical neutralizing epitopes and serves as an important vaccine target. Since RBD mutations occur in different MERS-CoV isolates and antibody escape mutants, cross-neutralization of divergent MERS-CoV strains...

Journal: :The Journal of allergy and clinical immunology 1997
J Schuurman G J Perdok T E Lourens P W Parren M D Chapman R C Aalberse

A chimeric human IgE monoclonal antibody was developed against the house dust mite allergen Der p 2. This chimeric antibody (hIgE-Dp2A) was composed of the heavy-chain variable domains and light chains of the original murine monoclonal antibody retaining its binding characteristics, whereas the heavy-chain constant domains were exchanged with the human IgE heavy chain. The chimeric IgE expressi...

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