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- 详细信息
- 文献和实验
- 技术资料
- 免疫原:
见官方网站
- 亚型:
见官方网站
- 形态:
液体或冻干粉
- 保存条件:
-20°C
- 克隆性:
多克隆
- 标记物:
见官方网站
- 适应物种:
见官方网站
- 保质期:
6个月
- 抗原来源:
见说明书
- 目录编号:
LK-104C
- 级别:
高
- 库存:
大量
- 供应商:
上海信裕生物科技有限公司
- 宿主:
见说明书
- 应用范围:
见官方网站
- 浓度:
见官方网站
- 靶点:
见官方网站
- 抗体英文名:
CaV1.2 Channel Antibody and Membrane Fractions Kit
- 抗体名:
CaV1.2 Channel Antibody and Membrane Fractions Kit
- 规格:
4 Vials
CaV1.2 Channel Antibody and Membrane Fractions Kit
Kit Contains Anti-CaV1.2 Antibody and all Controls Necessary for Robust Western Blot AnalysisCat #: LK-104C
4 Vials
CaV1.2 Channel Overexpressed Membrane Fractions (#LX-104) are Xenopus oocyte membrane fractions overexpressing CaV1.2 Channel. CaV1.2 Channel Overexpressed Membrane Fractions are your positive control for validating Alomone Labs CaV1.2 Channel Anti-CaV1.2 antibody (#ACC-003), Guinea pig Anti-CaV1.2 (#AGP-001) and Anti-CaV1.2a (#ACC-013).
Overexpressed Membrane Fractions are:
✓ Lyophilized powder
✓ Economical
✓ Shipped at room temperature (no need for dry ice and extra shipping costs)
✓ User-friendly & time-saving. Just add water, sample buffer and load your gel
- Compounds
- Scientific Background
- Related Products
| Product Name | Cat # | Size |
|---|---|---|
Guinea pig Anti-CaV1.2 |
AGP-001 | 1 x 0.2 ml |
CaV1.2 Channel Overexpressed Membrane Fractions |
LX-104 | 2 x 0.1 ml |
Note
Included with the products in this kit:
1 x 40 µg Guinea pig Anti-CaV1.2 control peptide antigen
1 x 0.1 ml lyophilized non-injected Xenopus oocyte overexpressed membrane fraction
Scientific Background
Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel1.
L-type Ca2+ channels make up one of three voltage-gated Ca2+ channel families. Four different α1 isoforms (CaV1.1 to CaV1.4) belong to the L-type subfamily. Structurally, each α1 subunit has four homologous domains (I-IV) and each domain has a six transmembrane section. Like many other voltage-gated channels, L-type Ca2+ channels have auxiliary subunits which are responsible for modulating the surface expression and properties of the channels2-5.
CaV1.1 is mostly expressed in the skeletal muscle, while CaV1.4 is mainly detected in the retina. The expression of both CaV1.2 and CaV1.3 is more extensive and includes neurons, heart, smooth muscle, inner ear, retina and pancreas6. L-type Ca2+ channels are involved in and modulate a variety of physiological functions such as muscle contraction, hormone secretion, neuronal excitability and gene expression5.
CaV1.2 undergoes various post-translational modifications. For example, it can undergo proteolytic cleavage at its C-terminal. This cleavage has been shown to take place in neurons following the activation of NMDA receptors5,7 and in the heart5,8,9. The cleaved moiety can still interact with the channel and its general purpose is to modulate channel activity5. Other postranslation modifications of the channel include phosphorylation of CaV1.2 by a number of kinases such as PKA, PKC, Src and CaMKII5. In addition, it is not surprising that phosphatases also regulate channel activity, as they are required to antagonize the activity of the various kinases known to phosphorylate CaV1.2 5.
The fact that CaV1.2 plays a prominent role in proper cardiac function has prompted endless studies regarding its regulation. Such studies have concluded that dysregulation of the channel leads to anomalies in heart contraction and thus heart failure5. Likewise, CaV1.2 defects have been detected in autism and bipolar disorder10.
References
- Bauer, C.S. et al. (2010) Curr. Opin. Neurobiol. 20, 563.
- Arikkath, J. et al. (2003) Curr. Opin. Neurobiol. 13, 298.
- Catterall, W.A. (2000) Annu. Rev. Cell. Dev. Biol. 16, 521.
- Davies, A. et al. (2007) Trends Pharmacol. Sci. 28, 220.
- Dai, S. et al. (2009) Physiol. Rev. 89, 411.
- Zuccotti, A. et al. (2011) Trends Pharmacol. Sci. 32, 366.
- Hell, J.W. et al. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 3362.
- De Jongh, K.S. et al. (1996) Biochemistry 35, 10392.
- Gao, T. et al. (2001) J. Biol. Chem. 276, 21089.
- Liao, P. et al. (2010) Pflugers. Arch. 460, 353.
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