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IgA exists in two isotypes, IgA1 and IgA2.They are both heavily glycosylated proteins. [9] While IgA1 predominates in serum (~80%), IgA2 percentages are higher in secretions than in serum (~35% in secretions); [10] the ratio of IgA1 and IgA2 secreting cells varies in the different lymphoid tissues of the human body: [11]
Selective immunoglobulin A (IgA) deficiency (SIgAD [1]) is a kind of immunodeficiency, a type of hypogammaglobulinemia. People with this deficiency lack immunoglobulin A (IgA), a type of antibody that protects against infections of the mucous membranes lining the mouth, airways, and digestive tract.
Dysgammaglobulinemia is a type of immune disorder characterized by a reduction in some types of gamma globulins, resulting in heightened susceptibility to some infectious diseases where primary immunity is antibody based.
[2] [6] [7] Photomicrograph of a histological section of human skin prepared for direct immunofluorescence using an anti-IgG antibody. The skin is from a patient with systemic lupus erythematosus and shows IgG deposit at two different places: The first is a band-like deposit along the epidermal basement membrane ("lupus band test" is positive).
Immunohistochemistry can be performed on tissue that has been fixed and embedded in paraffin, but also cryopreservated (frozen) tissue.Based on the way the tissue is preserved, there are different steps to prepare the tissue for immunohistochemistry, but the general method includes proper fixation, antigen retrieval incubation with primary antibody, then incubation with secondary antibody.
n/a Ensembl ENSG00000211895 n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) Chr 14: 105.7 – 105.71 Mb n/a PubMed search n/a Wikidata View/Edit Human Immunoglobulin heavy constant alpha 1 is a immunoglobulin gene with symbol IGHA1. It encodes a constant (C) segment of Immunoglobulin A heavy chain. Immunoglobulin A is an antibody that plays a critical role in ...
Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.
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