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Catalog Number: (BOSSBS-11040R-HRP)
Supplier: Bioss
Description: Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-CY7)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11040R-A750)
Supplier: Bioss
Description: Best vitelliform macular dystrophy, known as Best disease, is an early-onset autosomal dominant condition in which accumulation of lipofuscin-like material within and beneath the RPE leads to progressive loss of central vision. Best disease is frequently a reflection of mutations in the Bestrophin gene, which encodes a protein containing four putative transmembrane domains and localizes to the basolateral plasma membrane of RPE cells. Human Bestrophin forms oligomeric chloride channels that are sensitive to intracellular calcium. Missense mutations at the Bestrophin locus reduces or abolishes Bestrophin protein mediated membrane current. Bestrophin Bestrophin 2,Bestrophin 3, and Bestrophin 4 are transmembrane proteins that contain a high percentage of aromatic residues, a conserved RFP (Arg-Phe-Pro) motif and they function as anion channels.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-A647)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (SPCMSO155-500GM)
Supplier: Spectrum Chemical
Description: Sodium Chloride, Granular, USP is used in a variety of pharmaceutical formulations, to produce isotonic formulations, in tablet formulations and as an osmotic agent. This product is not sterile and not intended for use in the manufacture of injectable dosage forms, peritoneal dialysis solutions, hemodialysis solutions or hemofiltration solutions.
UOM: 1 * 500 g


Supplier: MP Biomedicals
Description: Chloride form quaternary ammonium functionality.Strongly basic, macroreticular resin of moderately high porosity with benzyltrialkylammonium functionality.

Catalog Number: (BOSSBS-11041R-A750)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterised channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Supplier: MP Biomedicals
Description: Cesium chloride, an inorganic compound, is an important source of cesium ions in a variety of applications. Its crystal structure forms a major structural type where each cesium ion is coordinated by 8 chlorine ions. Cesium chloride occurs naturally in mineral waters and as an impurity in carnallite (up to 0.002%), sylvite and kainite. Less than 20 tonnes of CsCl is produced annually worldwide, mostly from a cesium-bearing mineral pollucite.

Catalog Number: (BOSSBS-11041R-FITC)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-A555)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-A680)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterised channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-CY3)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-CY5)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-A488)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-A350)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11041R-HRP)
Supplier: Bioss
Description: The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
UOM: 1 * 100 µl


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