Human VAP-B Alexa Fluor® 488-conjugated 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: VAP-B

Vesicle-associated Membrane Protein (VAMP)-associated Protein B (VAP-B), also known as VAMP-B, is an ~30 Da ubiquitously expressed type IV transmembrane (TM) protein that belongs to the VAP family (1, 2). It is found in endoplasmic reticulum (ER), Golgi and other membranes as a homodimer or a heterodimer with VAP-A, probably associating through a GxxxG motif in the transmembrane regions (1, 2). Human VAP-B cDNA encodes 243 amino acids (aa) that include a 222 aa cytoplasmic domain and a 21 aa C-terminal membrane anchor. The cytoplasmic domain contains a mobile sperm protein (MSP) domain (aa 7‑124) plus a coiled-coil region (aa 159‑196) that initiates dimerization. Over aa 2-132, human VAP-B shares 97% aa sequence identity with mouse VAP-B and 81% aa sequence identity with VAP-A. VAP-A and VAP-B MSP domains recruit FFAT (two phenylalanines in an acidic tract)-motif-containing proteins to the cytosolic surface of ER membranes (2‑4). FFAT proteins mediate many of the effects of VAPs on regulation of membrane transport, phospholipid biosynthesis, microtubule organization, and the unfolded protein response (2, 3). VAPs also interact with some SNARE and viral proteins (2). A human polymorphism of VAP-B, P56S, is found in three familial motor neuron diseases, notably the amylotrophic lateral sclerosis variant ALS8 (2). It produces a non-functional protein that can dimerize with, and inhibit the function of, normal VAP-B, leading to formation of intracellular aggregates and increased ER-stress-induced death of motor neurons (5‑8). It can also promote cleavage and secretion of soluble VAP-B, which can then function as a ligand for EPH receptors (9). A naturally occurring 99 aa isoform of VAP-B that shows a 29 aa substitution for aa 71-243 is termed VAP-C (1, 10). It also appears to be a negative regulator of VAP-A and VAP-B (10). While VAP-B is used by hepatitis C virus (HCV) for its propagation, VAP-C inhibits HCV propagation (10).

Product Datasheets

Product Specific Notices

This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

Related Research Areas

• ALS Related Molecules
• Synaptic SNAREs