the right common carotid artery was exposed and then your external carotid artery was transected 2 mm distal from the carotid bifurcation after being ligated by 4 0 silk suture. The interior carotid artery was then isolated. The ICA and CCA were occluded with microvascular videos. A 3 cm size of 4 0 monofilament suture using a somewhat enlarged suggestion was introduced in to a hole in the ICA, and then the microvascular show in the ICA was eliminated. The suture was then gently advanced level about 18 mm in to the circle and ICA of Willis to cross the opening of the middle cerebral artery. The rat was sacrificed following the time course of ischemia, and the brain was exposed. Brain slices were stained with 2% triphenyl tetrazolium chloride to visualize Gossypol molecular weight and assess the infarct sizes in each class. The ischemic portion of the cerebral cortex and the portion of the normal cerebral cortex were removed for protein preparation. A set of oligonucleotide primers capable of amplifying the special cytoplasmic region of the human BAI3 log was used to enhance the corresponding region of the murine BAI3 mRNA. The resulting 524 bp amplification product was subcloned and sequenced to verify its identity. This fragment was then used to screen a brain lambda ZAP II cDNA library and several positive clones were obtained. Database searches with the deduced amino acid sequence revealed a high degree of identification between among positive clones and hBAI3. This murine cDNA fragment was then applied to rescreen the mouse brain cDNA library, and many Skin infection clones were isolated. Clone 107 had start codon, and clone 109 had a stop codon. The clones spanned a total of 4597 bp. Sequence analysis of the cDNA discovered an open reading frame which could direct the synthesis of a protein of 1522 amino acids, with a molecular mass of 171 kDa. The termination codon of the open reading frame was located at nucleotides 4567 4569. Database surveys identified a higher amount of deduced amino acid sequence identity between this cloned gene product and hBAI3 over the full length of the compound. According to this high level of homology, we revealed our cloned gene product as murine BAI3. The deduced amino acid sequences of the mBAI2, mBAI3 and mBAI1 genes are shown in Fig. 1. The TSR in the expanded extracellular domain and the STR are highly conserved included in this and located in the same positions. Nevertheless, the area of mBAI3 was divergent from Icotinib that of mBAI1 and mBAI2 genes. This divergence indicates that BAI interacting proteins that bind to this cytoplasmic area may vary among the three proteins. The presence of alternative splicing in the third cytoplasmic loop of the STR was confirmed by RT PCR. The expected structure of the mBAI3 protein includes prolonged extracellular and cytoplasmic domains, a GPS site, and an STR.