Bovine Immunoglobulin G, IgG ELISA Kit, E0010Bo

Immunoglubulin G (IgG) is a glycoprotein molecule which belongs to the immunoglobulin family of proteins known as antibodies. Immunoglobulins are the key component of humoral immunity. IgG is a monomeric immunoglobulin, built of two heavy chains gamma and two light chains. The heavy chains are linked to each other and to the light chain by disulfide bonds. Each molecule has two antigen binding sites. While the amino-terminal portions that exhibit highly variable amino-acid composition are involved in antigen binding, the C terminal constant parts are involved in complement binding, placental passage and binding to cell membrane.

Canine Immunoglobulin E, IgE ELISA Kit, E0208Ca

IgE is the class of antibodies produced in the lungs, skin, and mucous membranes. It may protect against parasite invasion, but it is a major factor in allergic reactions. The antigen-specific IgE interacts with mast cells and eosinophils, triggers the release of histamine, leukotrienes and other substances that lead to the itching, sneezing and congestion of allergies – and the life threatening respiratory distress of asthma and anaphylactic shock.

Rat Immunoglobulin A, IgA ELISA Kit, E0451Ra

IgA (immunoglobulin A) is a glycosylated protein of 160 kDa and is produced as a monomer or as a J chain linked dimer. Monomeric IgA constitutes 5-15 % of the serum immunoglobulins whereas dimeric IgA is localized to mucosa surfaces such as saliva, gastrointestinal secretion, bronchial fluids and milk. Mucosal IgA plays a major role in host defence by neutralising infectious agents at mucosal surfaces. The production is usually local and antigen specific IgA producing B cells can be found in regions under the lamina propria where they mature into dimeric IgA producing plasma cells. IgA deficiency is the most common immunodeficiency that may affect both serum and mucosal produced IgA. OR: The secretory component is a component of immunoglobulin A (IgA) which consists of a portion of the polymeric immunoglobulin receptor. Polymeric IgA binds to the polymeric immunoglobulin receptor on the basolateral surface of epithelial cells and is taken up into the cell via transcytosis. The receptor-IgA complex passes through the cellular compartments before being secreted on the luminal surface of the epithelial cells, still attached to the receptor. Proteolysis of the receptor occurs and the dimeric IgA molecule, along with the secretory component, are free to diffuse throughout the lumen.

Chicken Interferon γ, IFN-γ ELISA Kit, E0013Ch

Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

Human Hydroxyproline, Hyp ELISA Kit, E1900Hu

Hydroxyproline, a non-essential amino acid derived from proline, with no known therapeutic use. Hydroxproline is used as a major component of structural protiens such as collagen, connective tissues, plant cell walls, tendons and ligaments and provides skin elasticity. Vitiman C is required for the conversion process from proline to hydroxyproline, a deficincy in vitiman C can lead to defects in collagen synthesis, thus, resulting in easy bruising, internal bleeding, breakdown of connective tissue of the ligaments and tendons, and increased risk to blood vessel damage. An unusual feature of this amino acid is that, it is not incorporated into collagen during biosynthesis at the ribosomal level, but is formed from proline by a posttranslational modification by an enzymatic hydroxylation reaction.

Human Heat Shock 70kDa Protein 1A, HSPA1A ELISA Kit, E3015Hu

Function: In cooperation with other chaperones, the Hsp70 family stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Tissue specificity: HSPA1B is testis-specific.

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