Neurexin 1 (NRXN1) (AA 1063-1184) antibody

Details for Product No. ABIN968695
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Antigen
Synonyms CG7050, CT21808, Dmel\\CG7050, Nrx, Nrx1, dnrx, dnrx-1, nrx, NRXN1, Nrx-1, GB13455, GB18754, Nrxn1b, Hs.22998, PTHSL2, SCZD17, 1700062G21Rik, 9330127H16Rik, A230068P09Rik, mKIAA0578
Epitope
AA 1063-1184
(4), (2), (1), (1), (1)
Reactivity
Rat (Rattus)
(42), (36), (33), (28), (26), (13), (3)
Host
Mouse
(37), (5), (5), (1), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2)
Application
Western Blotting (WB)
(26), (22), (20), (14), (6), (6), (3), (1)
Pubmed 5 references available
Quantity 50 μg
Options
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Catalog No. ABIN968695
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Immunogen Rat Neurexin Ialpha
Clone 17
Isotype IgG1
Cross-Reactivity Mouse (Murine), Dog (Canine), Human
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Neurexin I
Background Neurexins are a family of neuron-specific cell surface proteins that contain hundreds of isoforms. These isoforms are generated from two different promoters in three different genes that code for many splice-variant transcripts. In rat, neurexins include 160-200 kDa alpha-neurexins and 90-100 kDa beta-neurexins, which include multipe isoforms identified as neurexin I, II, or III. Full-length alpha-neurexins contain three repeating domains that include a left arm (A) cell interaction module (LNS), a central EGF domain, and a right arm (B) LNS. beta-neurexins are identical to alpha-neurexins in the C-terminal region, but lack the five LNS repeats and three EGF domains of alpha -neurexins. Neurexin Ialpha was first characterized as a Ca2+-dependent receptor for alpha-latrotoxin, the excitatory neurotoxin in black widow spider venom. The C-terminus of Neurexin Ialpha interacts with the synaptic vesicle protein, synaptotagmin, while the three repeated sequences in the extracellular region have homology to cell adhesion-related proteins. Thus, Neurexin Ialpha may be important for cell-cell interactions and synaptic protein localization during the neuronal differentiation. This antibody is routinely tested by western blot analysis.
Molecular Weight 165 kDa
Comment

Related Products: ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Neurexin 1 (NRXN1) (AA 1063-1184) antibody Western blot analysis of Neurexin I on a P19 (murine embryonal carcinoma) lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti- Neurexin I antibody.
Product cited in: Ushkaryov, Petrenko, Geppert et al.: "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin." in: Science (New York, N.Y.), Vol. 257, Issue 5066, pp. 50-6, 1992 (PubMed).

Missler, Südhof: "Neurexins: three genes and 1001 products." in: Trends in genetics : TIG, Vol. 14, Issue 1, pp. 20-6, 1998 (PubMed).

Sugita, Khvochtev, Südhof: "Neurexins are functional alpha-latrotoxin receptors." in: Neuron, Vol. 22, Issue 3, pp. 489-96, 1999 (PubMed).

Hlubek, Stuenkel, Krasnoperov et al.: "Calcium-independent receptor for alpha-latrotoxin and neurexin 1alpha [corrected] facilitate toxin-induced channel formation: evidence that channel formation results from tethering of toxin to membrane." in: Molecular pharmacology, Vol. 57, Issue 3, pp. 519-28, 2000 (PubMed).

Fallon, Moreau, Croft et al.: "Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain." in: The Journal of biological chemistry, Vol. 277, Issue 1, pp. 486-91, 2002 (PubMed).

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