For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 6; NC_005105.3 (23843153..24482073, complement). Location: 6q12

NSO

Purified
80%, as determined by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin 1EU/ug (LAL).

Supplied as a lyophilized powder in PBS. Reconstitute with 500ul sterile PBS.

Lyophilized powder may be stored at -20 degree C. Stable for 12 months at -20 degree C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. Reconstituted product is stable for 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Small volumes of Nrxn1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Neurexin 1, also known as NRXN1A, is a neuronal type I transmembrane molecule that is encoded by one of three Neurexin genes (1, 2). Mature rat Neurexin 1 is a 130-200kD N- and O-glycosylated protein with a 1424 amino acid (aa) extracellular domain (ECD) and a 55 aa cytoplasmic region. The ECD contains six LNS domains interspersed with three EGF-like domains and a juxtamembrane O-glycosylation region; the cytoplasmic domain contains a PDZ recognition motif (1, 2). The ECD of rat Neurexin 1 shares 92% and 97% aa sequence identity with human and mouse Neurexin 1, respectively. It shares 68% aa sequence identity with rat Neurexin 2 and 3. Transcription of the Neurexin 1 gene from an internal promoter gives rise to Neurexin 1 which lacks the first five LNS domains and all of the EGF-like domains (3). Neurexins are combinatorially spliced at five canonical sites, giving rise to over 1000 potential isoforms (3, 4). This recombinant protein corresponds to the ECD of SwissProt #Q63372, isoform 13, which has short deletions at splice sites 1 and 2. Neurexin 1 is primarily expressed in the brain where it is localized to presynaptic terminals (3, 5). It binds black widow spider toxin -latrotoxin, plus dystroglycan, neurexophilin 1 and 3, and the postsynaptic neuroligins (6-9). The interaction between Neurexins and neuroligins is complex and is restricted to particular combinations of splice forms of each binding partner (9). These interactions promote the differentiation and maintenance of postsynaptic GABA and NMDA, but not AMPA terminals (10, 11). At presynaptic terminals, as well as in pituitary melanotrophs, alpha Neurexins are required for coupling voltage-dependent calcium channel signaling to neurotransmitter or hormone release (12-14).

Molecular Biology; MB-Neuroscience

SDS-PAGE: 165-175kD, reducing conditions.

154.7kD[Similar Products]

neurexin 1

neurexin 1; neurexin I-beta; neurexin-1-beta; neurexin I-alpha; neurexin-1-alpha; non-processed neurexin I-alpha

Neurexin-1

NRX1A_RAT

neuronal cell recognition molecule; may have a role in synaptogenesis [RGD, Feb 2006]

NRXN1: Cell surface protein involved in cell-cell-interactions, excytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)- triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their calcium-dependent interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latroxin from spider venom. Belongs to the neurexin family. 4 isoforms of the human protein are produced by alternative promoter.

Protein type: Membrane protein, integral; Receptor, misc.

Cellular Component: presynaptic membrane; cell surface; cell; endocytic vesicle; integral to membrane; plasma membrane; cell junction

Molecular Function: protein binding; calcium channel regulator activity; acetylcholine receptor binding; calcium ion binding; cell adhesion molecule binding; calcium-dependent protein binding; receptor binding

Biological Process: prepulse inhibition; neurotransmitter secretion; vocal learning; learning; social behavior; cerebellar granule cell differentiation; positive regulation of synaptic transmission, glutamatergic; negative regulation of filopodium formation; heterophilic cell adhesion; positive regulation of synaptogenesis; synaptic transmission; establishment of protein localization; synaptogenesis; ***** behavior; calcium-dependent cell-cell adhesion; protein heterotetramerization; neuron adhesion; angiogenesis; neuromuscular process controlling balance; cell adhesion; vesicle docking during exocytosis

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