Results 331 to 340 of about 235,597 (396)
Characterization of immunoglobulin heavy chain knockout rats [PDF]
European Journal of Immunology, 2010 AbstractThe rat is a species frequently used in immunological studies but, until now, there were no models with introduced gene‐specific mutations. In a recent study, we described for the first time the generation of novel rat lines with targeted mutations using zinc‐finger nucleases.
S. Ménoret +9 more
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Origins of immunoglobulin heavy chain domains
Journal of Molecular Evolution, 1980Using computer programs that analyze the evolutionary history and probability of relationship of protein sequences, we have investigated the gene duplication events that led to the present configuration of immunoglobulin C regions, with particular attention to the origins of the homology regions (domains) of the heavy chains.
Winona C. Barker +2 more
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The immunoglobulin heavy chain class switch
Molecular and Cellular Biochemistry, 1984While much has been learned concerning the molecular structural basis for the heavy chain class switch, many questions relating to the regulation of the switch remain unanswered, or at least controversial. Identification of the enzyme system which mediates the class switch, as well as other regulatory, possibly X-linked, genes should provide the ...
Max D. Cooper, Peter D. Burrows
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Veterinary clinical pathology, 2019
BACKGROUND Differentiation between neoplastic and reactive lymphocytic proliferations can be challenging in cats. PCR for antigen receptor rearrangements (PARR) testing is a useful diagnostic tool to assess clonality of a lymphoid population.
E. Rout +4 more
semanticscholar +1 more source
BACKGROUND Differentiation between neoplastic and reactive lymphocytic proliferations can be challenging in cats. PCR for antigen receptor rearrangements (PARR) testing is a useful diagnostic tool to assess clonality of a lymphoid population.
E. Rout +4 more
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International Journal of Immunogenetics, 1976
SUMMARYThe mobilities of murine splenocyte surface immunoglobulin heavy chains were compared by polyacrylamide gel electrophoresis in SDS‐containing buffers, with those of the heavy chains of human IgM, IgG, and IgD, and toad IgY. Human δ‐chain showed a mobility only slightly faster than that of human μ‐chain, and required double‐labelling techniques ...
Warr, G W, Marchalonis, J J
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SUMMARYThe mobilities of murine splenocyte surface immunoglobulin heavy chains were compared by polyacrylamide gel electrophoresis in SDS‐containing buffers, with those of the heavy chains of human IgM, IgG, and IgD, and toad IgY. Human δ‐chain showed a mobility only slightly faster than that of human μ‐chain, and required double‐labelling techniques ...
Warr, G W, Marchalonis, J J
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Production of Antisera to the Heavy Chains of Chicken Immunoglobulins
British Veterinary Journal, 1983A number of attempts made to raise monospecific antiserum against chicken immunoglobulin G in rabbits by conventional methods employing immunization with various whole IgG preparations, and complete Freund’s adjuvant resulted in antisera which showed reactivity predominantly against light chains.
Nandapalan, N. +2 more
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The role of immunoglobulin heavy chain binding protein
Immunology Today, 1987More than ten years ago a heavy chain binding protein (BiP) was described which is associated with immunoglobulin heavy chains (HC) within the endoplasmic reticulum (ER) [which is the site of Immunoglobulin (Ig) assembly]. Recently, Linda Hendershot and her collegues suggested that BiP might combine with nascent HC as they enter the ER and hold them ...
Linda Hendershot +2 more
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Regulation of immunoglobulin heavy‐chain gene rearrangements
Immunological Reviews, 2004Summary: Regulated assembly of antigen receptor gene segments to produce functional genes is a hallmark of B‐ and T‐lymphocyte development. The immunoglobulin heavy‐chain (IgH) and T‐cell receptor β‐chain genes rearrange first in B and T lineages, respectively.
Dipanjan Chowdhury, Ranjan Sen
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Hypervariable Region of Human Immunoglobulin Heavy Chains [PDF]
Nature New Biology, 1971 THE variable regions of human immunoglobulin light chains contain three areas of unusually high variability1–4. Similar hypervariable regions have been postulated for human heavy chains5, 6, but there are no amino-acid sequence data to support this idea.
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The origin of light and heavy chains of immunoglobulins
Biochemical and Biophysical Research Communications, 1971Abstract A model is proposed for the origin of H chains of Ig by the translocation of vc1 gene for light chains to a c2c3 gene giving rise to a vc1c2c3 gene. This explains why the common part of H chain is three times longer than the variable part.
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