Revision 1
#8575
Store at -20C
Calcium Ion Regulation Antibody Sampler Kit
1 Kit
(6 x 20 microliters)
877-616-CELL (2355)
877-678-TECH (8324)
3 Trask Lane | Danvers | Massachusetts | 01923 | USA
For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes | Product # | Quantity | Mol. Wt | Isotype/Source |
---|---|---|---|---|
ATP2A2/SERCA2 (D51B11) Rabbit mAb | 9580 | 20 µl | 114, 140 kDa | Rabbit IgG |
Phospho-Phospholamban (Ser16/Thr17) Antibody | 8496 | 20 µl | 6 (monomer); 12, 24 (oligomers) kDa | Rabbit |
Phospholamban (D9W8M) Rabbit mAb | 14562 | 20 µl | 12, 24 kDa | Rabbit IgG |
Phospho-PKA C (Thr197) (D45D3) Rabbit mAb | 5661 | 20 µl | 42 kDa | Rabbit IgG |
PKA C-α (D38C6) Rabbit mAb | 5842 | 20 µl | 42 kDa | Rabbit IgG |
ATP2A1/SERCA1 (D54G12) Rabbit mAb | 12293 | 20 µl | 100 kDa | Rabbit IgG |
Anti-rabbit IgG, HRP-linked Antibody | 7074 | 100 µl | Goat |
Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.
Description
Storage
Background
Phospholamban (PLN) was identified as a major phosphoprotein component of the SR (6). Despite very high expression in cardiac tissue, phospholamban is also expressed in skeletal and smooth muscle (7). Localization of PLN is limited to the SR, where it serves as a regulator of the sarco-endoplasmic reticulum calcium ATPase, SERCA (8). PLN binds directly to SERCA and effectively lowers its affinity for calcium, thus reducing calcium transport into the SR. Phosphorylation of PLN at Ser16 by PKA or myotonic dystrophy protein kinase and/or phosphorylation at Thr17 by Ca2+/calmodulin-dependent protein kinase results in release of PLN from SERCA, relief of this inhibition, and increased calcium uptake by SR (reviewed in 9,10). It has long been held that phosphorylation at Ser16 and Thr17 occurs sequentially, but increasing evidence suggests that phosphorylation, especially at Thr17, may be differentially regulated (reviewed in 11,12).
The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (13). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of the regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. Upon binding of cAMP to the R subunits, the auto-inhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (14). PKA phosphorylation is involved in the regulation of Ca2+ channels, including Cav1.1 in skeletal muscle and Cav1.2 in the heart (reviewed in 15).
Background References
- Hovnanian, A. (2007) Subcell Biochem 45, 337-63.
- Odermatt, A. et al. (1996) Nat Genet 14, 191-4.
- de Smedt, H. et al. (1991) J Biol Chem 266, 7092-5.
- Hawkins, C. et al. (1995) Mol Cell Biochem 142, 131-8.
- Viner, R.I. et al. (1999) Biochem J 340 ( Pt 3), 657-69.
- Kirchberber, M.A. et al. (1975) Recent Adv Stud Cardiac Struct Metab 5, 103-15.
- Fujii, J. et al. (1991) J Biol Chem 266, 11669-75.
- Tada, M. and Kirchberger, M.A. Recent Adv Stud Cardiac Struct Metab 11, 265-72.
- Traaseth, N.J. et al. (2008) Biochemistry 47, 3-13.
- Bhupathy, P. et al. (2007) J Mol Cell Cardiol 42, 903-11.
- Hagemann, D. and Xiao, R.P. (2002) Trends Cardiovasc Med 12, 51-6.
- Mattiazzi, A. et al. (2005) Cardiovasc Res 68, 366-75.
- Montminy, M. (1997) Annu Rev Biochem 66, 807-22.
- Dell'Acqua, M.L. and Scott, J.D. (1997) J Biol Chem 272, 12881-4.
- Dai, S. et al. (2009) Physiol Rev 89, 411-52.
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Revision 1
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