Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Alpha fetoproteins. --- Fetal globulins --- Fetoproteins, Alpha --- Fetuins --- Blood proteins --- Globulins --- Tumor proteins

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

This volume is THE definitive, completely up-to-date, reference work for ALL researchers and clinicians working in autoimmunity. Up-to-Date: This is a timely critical review of more than 100 autoantibodies by leading experts in their respective fields, and includes many recent references. International Experts: The 120 Chapters have been written by the top international cadre of authors who have provided structured, expert contributions. Comprehensive: A total comprehensive perspective on the processes which induce, inhibit or otherwise affect autoantibodies in human

Immunology. Immunopathology --- Autoantibodies. --- Autoimmune Diseases --- etiology. --- Immunoglobulins. --- Antibodies --- Immune globulins --- Immune serum globulin --- Blood proteins --- Globulins --- Plasma cells --- Antibody diversity --- Antigens --- Bacterial immunoglobulin-binding proteins --- Immunoglobulins --- Autoimmunity

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Lectins: Analytical Technologies covers both analytical and biological aspects of lectins (functional carbohydrate (complex sugar) recognition proteins) and provides researchers in the field with a resource containing background information and 'look-up' tables detailing lectin specificity and structures. Also included are methods and practical tips for designing new lectins from existing non-lectin proteins, automated approaches to lectin proteomics and high resolution mass spectrometry techniques. This book will be of interest to both novice and advanced researchers in biom

Lectins. --- Immunoglobulins. --- Antibodies --- Immune globulins --- Immune serum globulin --- Blood proteins --- Globulins --- Plasma cells --- Antibody diversity --- Antigens --- Bacterial immunoglobulin-binding proteins --- Protectins --- Receptor-specific proteins --- Hemagglutinin --- Immunoglobulins

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

This volume is a comprehensive collection of methods for the isolation, characterization, analysis and estimation of soluble lipoproteins. It surveys each aspect of lipoprotein technology in a critical manner which will enable the investigator to select the methods most relevant to his requirements. Having made his choice, he will then find a detailed description of how to perform the technique.

Analytical biochemistry --- Human biochemistry --- Clinical chemistry --- Pathological haematology --- Lipoproteins --- Blood lipoproteins --- blood --- Laboratory manuals --- Biochemistry --- Molecular biology --- Technique. --- Plasma lipoproteins --- Serum lipoproteins --- Blood lipids --- Blood proteins --- Lipoproteins - blood --- Lipoproteins - laboratory manuals --- Blood lipoproteins - Laboratory manuals

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

A vast number of neural cell surface glycoproteins belonging to the immunoglobulin superfamily have been isolated over the past two decades. In functional studies, many of them have been shown to confer adhesive properties to cells and to play an important role in developmental processes such as cell migration and axon outgrowth. Recent observations implicate Ig superfamily adhesion molecules in the regulation of activity-dependent synaptic plasticity, in regeneration after neural trauma, as well as in the pathogenesis of malformations in the developing nervous systems.

Immunoglobulins. --- Molecular neurobiology. --- Molecular neurology --- Nervous system --- Molecular biology --- Neurobiology --- Antibodies --- Immune globulins --- Immune serum globulin --- Blood proteins --- Globulins --- Plasma cells --- Antibody diversity --- Antigens --- Bacterial immunoglobulin-binding proteins --- Molecular aspects