Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Sequence and structure of V <sub>H</sub> domain from naturally occurring camel heavy chain immunoglobulins lacking light chains

1 Jan 1994

Abstract excerpt

We cloned 17 different PCR fragments encoding VH genes of camel (Camelus dromedarius). These clones were derived from the camel heavy chain immunoglobulins lacking the light chain counterpart of normal immunoglobulins. Insight into the camel VH sequences and structure may help the development of single domain antibodies. The most remarkable difference in the camel VH, consistent with the absence of the VL...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Blood groups and transfusion
Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 7831284
DOI: 10.1093/protein/7.9.1129

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Sequence and structure of V <sub>H</sub> domain from naturally occurring camel heavy chain immunoglobulins lacking light chainsPMID 7831284Read ↗

Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus speciesSemantic proximity Read ↗

Comparative Analysis of Immune Repertoires between Bactrian Camel's Conventional and Heavy-Chain AntibodiesSemantic proximity Read ↗

Single domain antibodies: comparison of camel VH and camelised human VH domainsSemantic proximity Read ↗

The Camel Adaptive Immune Receptors Repertoire as a Singular Example of Structural and Functional GenomicsSemantic proximity Read ↗

A Novel Promiscuous Class of Camelid Single-Domain Antibody Contributes to the Antigen-Binding RepertoireSemantic proximity Read ↗

The specific variable domain of camel heavy-chain antibodies is encoded in the germlineSemantic proximity Read ↗

The immunoglobulin A isotype of the Arabian camel ( <i>Camelus dromedarius</i> ) preserves the dualistic structure of unconventional single-domain and canonical heavy chainsSemantic proximity Read ↗

Production of Novel Recombinant Single-Domain Antibodies against Tandem Repeat Region of MUC1 MucinSemantic proximity Read ↗

Camelid Ig V genes reveal significant human homology not seen in therapeutic target genes, providing for a powerful therapeutic antibody platformSemantic proximity Read ↗

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining SiteSemantic proximity Read ↗

Variable fragments of heavy chain antibodies (VHHs): a new magic bullet molecule of medicine?Semantic proximity Read ↗

Fully Human VH Single Domains That Rival the Stability and Cleft Recognition of Camelid AntibodiesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.