Best2 Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	IHC, WB
Recommend Dilution	WB: 1:200-1:2000; IHC: 1:100-1:3000
Reactivity	Human, Rat
Host	Rabbit
Clonality	Polyclonal
Immunogen	Peptide (C)DPAQGYKDHTLD, corresponding to amino acid residues 259-270 of mouse Bestrophin-2. 3rd extracellular loop.
Formulation	Lyophilized. Concentration before lyophilization ~0.8mg/ml (lot dependent, please refer to CoA along with shipment for actual concentration). Buffer before lyophilization: Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.
Reconstitution Method	Add 50 ul double distilled water (DDW) to the lyophilized powder.
Purification	Affinity purified on immobilized antigen.
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Gene Name	bestrophin 2
Database Link	NP_001123666 Entrez Gene 54831 HumanEntrez Gene 364973 Rat UniProt ID Q8BGM5
Background	Mammalian Cl channels can be broadly classified into four different families: voltage-dependent Cl channels (CLCs), the cystic fibrosis transmembrane conductance regulator (CFTR), ligand-gated Cl channels (?-aminobutyric acid (GABA)) and glycine channels) and Ca2+-activated Cl channels (Bestrophin and Anoctamin channels). Bestrophins were first found by genetic linkage of human-Bestrophin-1 (hBest1) to a juvenile form of macular degeneration called Best vitelliform macular dystrophy. To date Bestrophin 1-4 have been identified, although Bestrophin-3 and Bestrophin-4 have been observed only at the RNA level. In addition, splice variants of some of these Ca2+-activated Cl channels (CaCCs) have also been detected. CaCCs are known to be involved in the regulation of olfaction, taste, phototransduction, and excitability in the nervous system. However, the molecular identity and functional role of CaCC in the brain have not been well established. Bestrophin-2 is prominently expressed in colon and testes. Recently, Bestrophin-2 has also been found to be expressed in olfactory sensory neurons (OSNs). Two different topologies for Bestrophin-1 have been proposed. The first structure proposes that six hydrophobic domains span the membrane, while the second suggests that there are only four membrane-spanning domains. The same structural controversy applies to Bestrophin-2. Bestrophin-1 and Bestrophin-2 (as well as Bestrophin-4 by heterologous expression) are activated by intracellular Ca2+. Ca2+-dependent activation of Bestrophin-2 was also demonstrated in Xenopus.
Synonyms	FLJ20132; VMD2L1
Reference Data

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