|Application ||WB, IHC, FC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||173297 Da|
|Homology||Rat, human - identical|
|Other Names||Brain-specific angiogenesis inhibitor 1, Bai1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)GRVRTYQFDSFLESTR, corresponding to amino acid residues 97-112 of mouse BAI1 (Accession Q3UHD1). Extracellular, N-terminus.The antibody will recognize the intact BAI1 receptor as well as the proteolytically processed N-terminal fragment. This fragment is also known as Vasculostatin (Vstat120).|
|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.
The three members of the brain angiogenesis inhibitor (BaI1-3) are receptors belonging to the adhesion subfamily of G-protein coupled receptor superfamily. Like all members of GPCRs, all three BaIs have seven transmembrane domains, an intracellular C-terminal tail and extracellular N-terminus. Like other adhesion members, the N-terminus is quite large1,2. Many domains are localized to the N-terminus; various glycosylations sites are present, there is a GPCR proteolysis site, a putative hormone binding domain and thrombospondin type 1 repeats which regulate the anti-angiogenic activity of thrombospondin-12,3. The C-terminal tail interacts with PDZ-domain proteins. Unique to BaI1 is a proline-rich domain required for interacting with Src homology domains and WW domain proteins2,4. Like most adhesion GPCRs, BaI also undergo proteolysis at the N-terminus at a highly rich cystein domain2. Following autocleavage, the N-terminal fragment remains associated to the receptor. In BaI1, proteolysis yields a partly secreted 120 kDa. fragment (vasculostatin-120) or a 40 kDa. fragment both having antiangiogenic effects2,5. At the mRNA level, all BaIs are expressed in fetal and adult human brain2,6. BaI2 is detected in the human heart and skeletal muscle. BaI3 is expressed in the human heart, testis and small intestine. In mouse, both BaI2 and BaI3 are restricted to the brain2. These receptors are implicated in various diseases and disorders such as primary glioma, pulmonary adenocarcinomas, gastric and colorectal cancers2,6,7. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of mouse BaI1. Anti-Bai1 (extracellular) antibody (#AG1364) can be used in western blot and indirect flow cytometry applications. It has been designed to recognize Bai1 from rat, mouse, and human samples.
1. Park, D. et al. (2007) Nature 450, 430.
2. Cork, S.M. et al. (2011) J. Mol. Med. 89, 743.
3. de Fraipont, F. et al. (2001) Trends Mol. Med. 7, 401.
4. Oda, K. et al. (1999) Cytogenet. Cell. Genet. 84, 75.
5. Cork, S.M. et al. (2011) Oncogene doi: 10.1038/onc.2012.1.
6. Shiratsuchi, T. et al. (1997) Cytogenet. Cell. Genet. 79, 103.
7. Hatanaka, H. et al. (2000) Int. J. Mol. Med. 5, 181.
8. Fukushima, Y. et al. (1998) Int. J. Oncol. 13, 967.
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