|Application ||WB, IHC|
|Calculated MW||47151 Da|
|Homology||Mouse - identical; human - 11/14 amino acid residues identical.|
|Other Names||Somatostatin receptor type 3, SS-3-R, SS3-R, SS3R, SSR-28, Sstr3|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide KVRSTTRRVRAPSC, corresponding to amino acid residues 233-246 of rat SSTR3 (Accession# P30936). Intracellular, between transmembrane domains 5 and 6.|
|Peptide Confirmation||Confirmed by amino acid analysis and massspectrography.|
|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 water.|
|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.
Somatostatin (SST) is a small cyclic peptide that was first identified as a powerful inhibitor of the secretion of various hormones including growth hormone (GH), thyroid-stimulating hormone (TSH) and prolactin from the pituitary, as well as practically every major hormone from the intestinal tract. SST consists of two major bioactive forms, SST-14 and the N-terminus extended peptide SST-28 that can be produced by a wide variety of neuroendocrine, inflammatory and immune cells. SST induces in target cells a variety of physiological functions that include nueromodulation, cell secretion, cell proliferation and smooth muscle contractility. SST acts on its multiple cell targets via a family of six receptors that are originated form five genes: SSTR1, SSTR2a, SSTR2b, SSTRR3, SSTR4, SSTR5. The SSTRs are members of the G-protein coupled receptor superfamily and they modulate cell response via multiple second messenger systems such as inhibition of adenylate cyclase, modulation of conductance of ion channels and protein dephosphorylation. SSTRs are expressed widely in both the brain and peripheral tissues but with receptor subtype variations between the different cell types. Thus, SSTR3 expression in the brain is primarily concentrated in the cerebellum with lesser expression in peripheral organs such as the spleen, the liver and the pituitary. Strong SSTR expression has been detected in a variety of human tumors including pancreatic, breast, lung and prostate cancers. In fact, SST has been shown to inhibit the growth of various normal and tumor cells. On this basis several long lasting SST analogs have been developed and are being tested for use in several pathologies such as various cancers, acromegaly, immunoproliferative disorders, diabetic retinopathy, epilepsy and pain. Abgent is pleased to offer a highly specific antibody directed against a highly conserved epitope in the third intracellular loop of the rat SSTR3. Anti-Somatostatin Receptor Type 3 antibody (#AG1019) can be used in western blot analysis and immunohistochemical applications, and will also recognize SSTR3 in mouse and rat samples .
1. Patel, Y.C. (1999) Fron. Neuroendocrin. 20,157.
2. Weckbecker, G. et al. (2003) Nat. Rev. Drug Disc. 2, 999.
3. Culler, M.D. et al. (2002) Ann. Endocrinol. (Paris) 63, 2S5.
4. Corleto, V.D. et al. (2004) Dig. Liver Dis. 36, S8.
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