|Application ||WB, IHC, ICC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||43435 Da|
|Homology||Mouse, dog - identical; rat - 15/16 amino acid residues identical.|
|Other Names||Neuromedin-B receptor, NMB-R, Epididymis tissue protein Li 185a, Neuromedin-B-preferring bombesin receptor, NMBR|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)KSAHNLPGEYNEHTKK, corresponding to amino acid residues 241-256 of human BB1 (Accession P28336). 3rd intracellular loop.|
|Peptide Confirmation||Confirmed by 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||0.6 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% 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.
Bombesin receptor 1 (BB1) is a member of a family of receptors that binds the 14 amino acid peptide bombesin. Bombesin was initially isolated from frog skin and it was later established that mammals express endogenous bombesin-like peptides such as gastrin-releasing peptide (GRP) and neuromedin B (NMB), 27 and 10 amino acid homologues, respectively.1 BB1 is the preferred receptor for NMB (therefore it is also known as NMB receptor) while BB2 is the preferred receptor for GRP.2 BB3 was the third member of the bombesin family of receptors to be cloned based upon its sequence similarity to BB1 and BB2.1 The affinity of BB3 for bombesin is lower than that of the BB1 and BB2 receptors, as are its affinities for NMB and GRP. This suggests that the endogenous mammalian ligand for the BB3 receptor remains to be identified. All three bombesin receptors are members of the 7-transmembrane domain, G protein-coupled receptor (GPCR) superfamily. BB1 is coupled to a Gq/11 protein that activates phospholipase C (PLC) and leads to production of inositol 1,4,5-trisphosphate (InsP3), intracellular Ca2+ mobilization, and cell growth.1 BB1 is expressed in the brain where it likely mediates the inhibition of food intake and regulates the stress and fear response. BB1 and its ligand NMB are expressed in the pituitary where they participate in the regulation of thyroid-stimulating hormone (TSH) secretion in both autocrine and paracrine fashions.3 In the periphery, BB1 is expressed in the gastrointestinal and urogenital smooth muscle but its physiological function in these tissues is unclear. Finally, BB1 is over-expressed in several human tumors especially colon and non-small lung cancer where it acts as a growth factor receptor inducing tumor growth. BB1 is considered a potential target for the development of both diagnostics and anti-cancer therapies.4 Abgent is pleased to offer a highly specific antibody directed against a well conserved epitope located in the 3rd intracellular loop of the human BB1 receptor. Anti-Bombesin Receptor 1 antibody (#AG1367) can be used in western blot and immunocytochemical applications, and will recognize BB1 from human, rat, mouse, and dog samples.
1. Ohki-Hamazaki, H. et al. (2005) Int. J. Dev. Biol. 49, 293.
2. Wada E. et al. (1991) Neuron 6, 421.
3. Oliveira, K.J. et al. (2006) J Mol Endocrinol 36, 73.
4. Reubi, J.C. (2003) Endocr. Rev. 24, 389.
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