|Application ||WB, LCI|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||166615 Da|
|Homology||Mouse, human- identical.|
|Other Names||Latrophilin-1, Calcium-independent alpha-latrotoxin receptor 1, CIRL-1, Lphn1, Cirl, Cirl1, Cl1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide CEPREVRRVQWPATQ(G), corresponding to amino acid residues 480-494 of rat Latrophilin-1 (Accession O88917).ֲ Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis and mass-spectrography.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl DDW.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Latrophilins (Latrophilin1-3) are members of the adhesion G-protein coupled receptor subfamily. Like all GPCRs, Latrophilins have seven transmembrane domains and are distinguished by a large extracellular N-terminal tail and a large intracellular C-terminal tail1. The N-terminus has several cell adhesion domains and undergoes proteolysis after synthesis, while the C-terminal has various consensus post-translational sites like phosphorylation and palmitoylation2. In addition, Latrophilins undergo alternative splicing3. Latrophilin-1 was discovered by its ability to bind α-Latrotoxin (α-LTX), a toxin isolated from the black widow spider venom4. α-LTX induces exocytosis by creating a Ca2+ influx in the presynaptic membrane. α-LTX can also stimulate small vesicle exocytosis in a Ca2+ independent manner. Three receptors have been found to bind α-LTX. Of the three, Latrophilins are responsible for the Ca2+-independent effects of α-LTX2. The binding of α-LTX to Latrophilin-1 increases exocytosis of neurotransmitters5,6. In an attempt to find the natural ligand of Latrophilin-1, Lasso, a splice variant of Teneneurin-2 was discovered to be an endogenous binding partner of the adhesion-GPCR7. Teneneurins are large glycoproteins with a single transmembrane domain8,9. Like Latrophilin-1, Teneneurins are mostly expressed in the brain where they modulate neurite outgrowth, axon guidance and synaptogenesis7. Regarding the localization of Latrophilins, Latrophilin-1 is expressed predominantly in the brain, Latrophilin-2 is highly expressed in the liver and lung, while Latrophilin-3 is almost exclusively detected in the brain1,10. Abgent is pleased to offer a highly specific antibody directed against an epitope of rat Latrophilin-1. Anti-Latrophilin-1 (extracellular) antibody (#AG1220) can be used in western blot, immunohistochemistry and immunocytochemistry applications and was designed to recognize Latrophilin-1 from rat and mouse samples.
References 1. Sugita, S. et al. (1998) J. Biol. Chem. 273, 32715. 2. Martinez, A.F. et al. (2011) Am. J. Med. Genet. Part B 156, 1. 3. Matsushita, H. et al. (1999) FEBS Lett. 443, 348. 4. Davletov, B.A. et al. (1996) J. Biol. Chem. 271, 23239. 5. Capogna, M. et al. (2003) J. Neurosci. 23, 4044. 6. Lelyanova, V.G. et al. (2009) Bull. Exp. Biol. Med. 1017, 701. 7. Silva, J.P. et al. (2011) Proc. Natl. Acad. Sci. U.S.A. 108, 12113. 8. Levine, A. et al. (1994) Cell 77, 987. 9. Tucker, R.P. and Chiquet-Ehrismann, R. (2006) Dev. Biol. 290, 237. 10. Ichtchenko, K. et al. (1999) J. Biol. Chem. 274, 5491.
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