Human Serum Albumin Antibody Summary
This antibody functions as an ELISA capture antibody when paired with Mouse Anti-Human Serum Albumin Monoclonal Antibody (Catalog # MAB14551).
This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human Serum Albumin DuoSet ELISA Kit (Catalog # DY1455) for convenient development of a sandwich ELISA.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Human Albumin ELISA Standard Curve. Recombinant Human Albumin protein was serially diluted 2-fold and captured by Mouse Anti-Human Serum Albumin Monoclonal Antibody (Catalog # MAB14552) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human Serum Albumin Monoclonal Antibody (Catalog # MAB14551) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Albumins are a family of globular proteins, the most common of which are serum albumins. Albumins are commonly found in blood plasma, and are unique from other blood proteins in that they are not glycosylated. Albumin is a 65-70 kDa protein with serum albumin being the main protein of human blood plasma. It binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin, thyroxine (T4) and pharmaceuticals (including barbiturates) - its main function is to regulate the colloidal osmotic pressure of blood. Albumin comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds.
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