Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

Hyaluronic Acid Binding Protein bovine may be used for incubation of specimens for immunofluorescence analysis of human megakaryocytes.

Biochem/physiol Actions

Hyaluronic Acid Binding Protein (HABP) levels increases during oocyte maturation and it promotes cumulus expansion during in vitro maturation.

In addition to being an important structural component of tissues in all vertebrates, HA is also associated with several biological functions including intracellular signaling.

May be useful in hyaluronic acid binding or detection.

General description

Karl Meyer and John Palmer first isolated hyaluronic acid (HA) from the vitreous of bovine eyes. They coined the name “hyaluronic acid” as a conjugation of two words, hyaloid (vitreous) and uronic acid. HA has an extended random coil structure in physiological solution. Due to its random-coil structure and high molecular weight (HMW), HA forms very viscose and elastic solution with a huge hydrodynamic volume.

Hyaluronic acid (HA) is a linear polysaccharide consisting of a repeating disaccharide of N-acetyl D-glucosamine (GlcNAc) and D-glucuronic acid (GlcA) with 1→4 interglycosidic linkages and these disaccharide repeating units are in turn linked by β (1→3) linkages. The number of repeating disaccharides in a HA molecule ranges from 2,000 to 25,000, which relates to a molecular mass of 106-107. The unique biological roles of HA is mainly due to the specific binding and interaction with HA-binding proteins also known as hyaladherins. Most hyaladherins is composed of a specific binding domain, also called a link module, which is composed of two α-helices and two antiparallel β-sheets.