| 货号 | ACC-106-50ul |
| 描述 | Each antibody ordered from Alomone Labs is supplied with its corresponding control peptide (antigen), free of charge. A Rabbit Polyclonal Antibody to Cavβ1 Subunit |
| 反应种属 | M, R |
| 应用 | IH, WB |
| 供应商 | Alomone |
| 背景 | Voltage-gated Ca2+(CaV) channels are ubiquitously expressed and function as Ca2+ conducting pores in the plasma membrane1. Based on their electrophysiological and pharmacological properties, CaV channels have traditionally been classified into L, T, N, P, Q, and R types2. L-type Ca2+ channels are heteromultimers composed of four independently encoded proteins, the pore-forming α1 subunit, which triggers Ca2+ flow across the membrane, and the subunits α2δ, γ, and β3. CaVβ subunits play critical roles in membrane trafficking of the channel complex and regulation of voltage-dependent gating. The CaVβ subunit binds to the endoplasmic reticulum (ER) retention signal in the I-II loop of the α1-subunit, which allows channels to traffic to the surface membrane4. Furthermore, CaVβ subunits not only allow for membrane trafficking of the channel complex, they also can play a role in determining the subcellular localization of channels on the surface membrane5. There are four distinct CaVβ subunits CaVβ1, CaVβ2, CaVβ3 and CaVβ46. Three splice variants exist for the β1 subunit: β1a, β1b and β1c. β1a is known to be expressed in skeletal muscle and brain, but not in smooth muscle or heart. β1a appears to be important for the functional expression of the α1 subunit in skeletal muscle7. β1b was identified by cloning in rat brain, heart and hippocampus, and differs from β1a by having a deletion of ~50 amino acids at residue 209, and having a 120-residue C-terminal elongation. β1c was cloned from human heart and hippocampus and has the same deletion as β1b, but lacks the C-terminal extension. |
| 运输条件 | Ambient |
| 存放说明 | -20 |
| 纯度 | Affinity purified on immobilized antigen. |
| 参考文献 | 1.Catterall, W.A.et al. (2000) Annu. Rev. Cell. Dev. Biol.16,521. 2.Qin, N.et al.(2002)Mol. Pharmacol.62,485. 3.De Jongh, K.S.et al.(1990) J. Biol. Chem. 265,14738. 4.Bichet, D.et al. (2000) Neuron25,177. 5.Foell, J.D.et al.(2004)Physiol. Genomics 17,183. 6.Dolphin, A.C.(2003) J. Bioenerg. Biomembr.35,599. 7.Beurg, M.et al.(1999) Biophys J.77,2953. |
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