Rat Agrin Antibody

Applications

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.

Preparation and Storage

Background: Agrin

Agrin is a 400-600 kDa heparan sulfate proteoglycan component of the extracellular matrix. The N-terminal half of rat Agrin, which mediates ECM interactions, contains nine Kazal-type protease inhibitor domains, two Laminin EGF-like domains, and one SEA domain. The C-terminal half contains four EGF-like repeats and three Laminin globular G domains. Human Agrin also contains a Laminin-binding N-terminal Agrin domain (NtA), and mouse and chick Agrin include the NtA domain only by the use of an alternate promoter. Additional isoforms are generated by alternate splicing at sites Y and Z in the C-terminal half of rat Agrin (known as A and B, respectively in chick). Agrin isoforms that contain an insert at site Z (Z+ forms) are known as neural Agrin and are selectively produced by motoneurons. Other isoforms are known as muscle Agrin and are additionally expressed in non-neuronal tissues, particularly in basement membranes of the lung and kidney (1‑3). This recombinant protein consists of the C-terminal half of rat Agrin and contains a nine amino acid (aa) insert at the Z site. It shares 59%, 80%, and 94% aa sequence identity with comparable regions of chick, human, and mouse Agrin, respectively. The C-terminal half of Z- and Z+ Agrin binds to alpha -Dystroglycan and mediates adhesion between motoneurons and myotubes at the neuromuscular junction (NMJ) (4‑6). In contrast, only Z+ Agrin is effective at inducing clustering of the postsynaptic Acetylcholine Receptor (AChR) and presynaptic motoneuron differentiation (7, 8). Agrin-induced AChR clustering requires a myotube receptor complex that contains alpha -Dystroglycan, MuSK, and LRP4 (4, 9‑11). Agrin exhibits many functions in addition to NMJ development. It is enriched in senile Alzheimer’s disease plaques where it binds the A beta (1-40) peptide and promotes amyloid fibril formation (12). It regulates neuronal excitability by binding and inhibiting the alpha 3 subunit of the neuronal Na/K ATPase (13). It functions as an epithelial cell attachment receptor for HIV-1 through interactions with the gp41 coat protein (14). During T cell activation, Agrin contributes to formation of the immunological synapse and regulates the threshold of T cell activation (15).

Product Datasheets

Related Research Areas

• Extracellular Matrix Molecules
• Proteoglycans
• Synaptic Proteins