|Application ||WB, LCI|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||51547 Da|
|Homology||Human - 13/14 amino acid residues identical; rat, mouse - 12/14 amino acid residues identical.|
|Other Names||Vasoactive intestinal polypeptide receptor 1, VIP-R-1, Pituitary adenylate cyclase-activating polypeptide type II receptor, PACAP type II receptor, PACAP-R-2, PACAP-R2, VPAC1, VIPR1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)EEAQLENETIG(S)SK, corresponding to amino acid residues 52-65 of human VPAC1 (Accession P32241). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|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.
Vasointestinal peptide (VIP) and pituitary adenylate cyclase–activating peptide (PACAP) belong to the glucagon hormone superfamily, which includes secretin, growth hormone–releasing hormone (GHRH), glucagon, glucagon-like peptides 1 and 2 (GLP-1 and GLP-2), peptide histidine methionine (PHM), and glucose-dependent insulinotropic polypeptide (GIP)1. PACAP and VIP effects have been described in the digestive tract, cardiovascular system, airways, reproductive system, immune system, endocrine glands, and brain2. VIP and PACAP share a common G-protein coupled receptor, VPAC13. VPAC1 is a membrane-associated protein and shares significant homology with members of the G-protein coupled class B receptor family, the most important of which is the presence of large N-terminal extracellular domains which contain 10 highly conserved amino acids including six cysteines, putative N-terminal leader sequences and several potential N-glycosylation sites4. In the CNS, VPAC1 receptors are abundantly localized in piriform cortex, cerebral cortex, suprachiasmatic nucleus, hippocampus, and pineal gland5. In peripheral tissues, VPAC1 receptors have been found in breast, kidney, liver, lung, prostate, spleen, and mucosa of the gastrointestinal tract6. VPAC1 mediates a large array of VIP and PACAP actions on exocrine secretion, hormones release, muscle relaxation, metabolism, fetus growth, tumor cells and embryonic brain development7. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of human VPAC1. Anti-VPAC1 (extracellular) antibody (#AG1002) can be used in western blot, immunohistochemistry, immunocytochemistry and indirect flow cytometry applications and has been designed to recognize VPAC1 from mouse, rat and human samples.
References 1. Vaudry, D. et al. (2000) Pharm. Rev. 52, 269. 2. Gozes, I. et al. (2003) Curr Pharm Des. 9, 483. 3. Laburthe, M. et al. (2002) Receptors Channels 8, 137. 4. Laburthe, M. et al. (1996) Ann. N. Y. Acad. Sci. 805, 94. 5. Usdin, T. et al. (1994) Endocrinology 135, 2662. 6. Reubi, J. C. et al. (2000). Ann. N. Y. Acad. Sci. 9, 211. 7. Said, S. I. et al. (1991) Trends Endocrinol. Metab. 2, 107.
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