Human ELFN1 Alexa Fluor® 594-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: ELFN1

ELFN1 (Extracellular leucine-rich repeat and fibronectin type-III domain-containing protein 1), also known as Protein phosphatase 1 regulatory subunit 28, is a member of the extracellular Leucine-Rich Repeat superfamily (1). Expressed mainly in the nervous system, ELFN1 is a transmembrane protein that inhibits the activity of protein phosphatase 1 (PP1) complexes (2). Mature human ELFN1 consists of a 391 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment and a 389 aa cytoplasmic tail. The ECD includes one fibronectin type-III domain, six leucine-rich repeats (LRR) and one LRR C-terminal (LRRCT) domain. Human ELFN1 shares 90% aa sequence identity with mouse and rat ELFN1. The cytoplasmic tail contains many tyrosine but no other detectable motifs. ELFN1 is strongly expressed in globus pallidus and interneurons in cortex and hippocampus in both developing and adult brains (1). It is also expressed in endocrine and reproductive tissues (1). Given the functions and discrete patterns of many known LRR family proteins, it has been proposed that ELFN1 could serve as a neuronal adhesion molecule and play an integral role in synapse formation and differentiation via the coordination of both pre- and postsynaptic machineries, thereby involved in neurite outgrowth, axon guidance, fasciculation, and synapse formation (3). Recent studies showed that ELFN1 physically anchor metabotropic glutamate receptor 6 (mGluR6) and mGluR7 across retinal and hippocampal synapses (3-4), and can be recruited selectively to all group III mGluRs (mGluR4, mGluR6, mGluR7, and mGluR8) to allosterically modulate these receptors (5).

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

• Phosphatases and Regulators
• Synaptic Proteins