Ca_V1.2 Channel Antibody and Membrane Fractions Kit

Ca_V1.2 Channel Overexpressed Membrane Fractions (#LX-104) are Xenopus oocyte membrane fractions overexpressing Ca_V1.2 Channel. Ca_V1.2 Channel Overexpressed Membrane Fractions are your positive control for validating Alomone Labs Ca_V1.2 Channel Anti-Ca_V1.2 antibody (#ACC-003), Guinea pig Anti-Ca_V1.2 (#AGP-001) and Anti-Ca_V1.2a (#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

Included with the products in this kit:
1 x 40 µg Guinea pig Anti-Ca_V1.2 control peptide antigen
1 x 0.1 ml lyophilized non-injected Xenopus oocyte overexpressed membrane fraction
Scientific Background 

Voltage-gated Ca²⁺ channels (Ca_V), 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 (Ca_V1.1 to Ca_V1.4) 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 channels^2-5.

Ca_V1.1 is mostly expressed in the skeletal muscle, while Ca_V1.4 is mainly detected in the retina. The expression of both Ca_V1.2 and Ca_V1.3 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.

Ca_V1.2 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 receptors^5,7 and in the heart^5,8,9. 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 Ca_V1.2 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 Ca_V1.2 ⁵.

The fact that Ca_V1.2 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, Ca_V1.2 defects have been detected in autism and bipolar disorder¹⁰.

1. Bauer, C.S. et al. (2010) Curr. Opin. Neurobiol. 20, 563.
2. Arikkath, J. et al. (2003) Curr. Opin. Neurobiol. 13, 298.
3. Catterall, W.A. (2000) Annu. Rev. Cell. Dev. Biol. 16, 521.
4. Davies, A. et al. (2007) Trends Pharmacol. Sci. 28, 220.
5. Dai, S. et al. (2009) Physiol. Rev. 89, 411.
6. Zuccotti, A. et al. (2011) Trends Pharmacol. Sci. 32, 366.
7. Hell, J.W. et al. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 3362.
8. De Jongh, K.S. et al. (1996) Biochemistry 35, 10392.
9. Gao, T. et al. (2001) J. Biol. Chem. 276, 21089.
10. Liao, P. et al. (2010) Pflugers. Arch. 460, 353.