Product Pathways - Ca / cAMP / Lipid Signaling
Phospho-Phospholamban (Ser16/Thr17) Antibody #8496
|8496S||100 µl (10 western blots)||---||In Stock||---|
|8496||carrier free and custom formulation / quantity||email request|
Already purchased this product? Write a Review.
|W||1:1000||Rat||Endogenous||6 (monomer); 12, 24 (oligomers)||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Human, Mouse, Bovine, Dog, Pig.
Specificity / Sensitivity
Phospho-Phospholamban (Ser16/Thr17) Antibody recognizes endogenous levels of phospholamban protein only when phosphorylated at Ser16 and Thr17. This antibody does not detect mono- or non-phosphorylated phospholamban.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser16/Thr17 of human phospholamban protein. Antibodies are purified by protein A and peptide affinity chromatography.
Phospholamban (PLN) was identified as a major phosphoprotein component of the sarcoplasmic reticulum (SR) (1). Its name, "lamban", is derived from the greek word "lambano" meaning "to receive", so named due to the fact that phospholamban is heavily phosphorylated on serine and threonine residues in response to cardiac stimulation (1). Although originally thought to be a single 20-25 kDa protein due to its electrophoretic mobility on SDS-PAGE, PLN is actually a 52 amino acid, 6 kDa, membrane-spanning protein capable of forming stable homooligomers, even in the presence of SDS (2). Despite very high expression in cardiac tissue, phospholamban is also expressed in skeletal and smooth muscle (3). Localization of PLN is limited to the SR, where it serves as a regulator of the sarco-endoplasmic reticulum calcium ATPase, SERCA (4). 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 Protein Kinase A 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 the SR (reviewed in 5,6). 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 7,8).
Rodent models of heart failure have shown that the expression level and degree of phosphorylation of PLN are critical in modulating calcium flux and contractility (reviewed in 9-11). Deletion or decreased expression of PLN promotes increased calcium flux and increased cardiac contractility, whereas overexpression of PLN results in sequestration of SERCA, decreased calcium flux, reduced contractility, and rescue of cardiac dysfunction and failure in mouse models of hypertension and cardiomyopathy (reviewed in 10). Distinct mutations in PLN have been detected in humans, resulting either in decreased or no expression of PLN protein (12,13) or binding defects between PLN, SERCA and/or regulatory proteins (14,15), both of which result in cardiac myopathy and heart failure. Interestingly, while the human phenotype of most PLN defects mimic those seen in rodent and vice versa, there are some instances where the type and severity of cardiac disease resulting from PLN mutations in rodent and human differ, making a consensus mechanism elusive.
- Kirchberber, M.A. et al. (1975) Recent Adv Stud Cardiac Struct Metab 5, 103-15.
- Zhan, Q.Q. et al. (1991) J Biol Chem 266, 21810-4.
- 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.
- Chu, G. and Kranias, E.G. (2006) Novartis Found Symp 274, 156-71; discussion 172-5, 272-6.
- Schwinger, R.H. and Frank, K.F. (2003) Sci STKE 2003, pe15.
- MacLennan, D.H. and Kranias, E.G. (2003) Nat Rev Mol Cell Biol 4, 566-77.
- Haghighi, K. et al. (2008) Hum Mutat 29, 640-7.
- Haghighi, K. et al. (2003) J Clin Invest 111, 869-76.
- Schmitt, J.P. et al. (2003) Science 299, 1410-3.
- Haghighi, K. et al. (2006) Proc Natl Acad Sci USA 103, 1388-93.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
- 4274 ATP2A1/SERCA1 (A988) Antibody
- 4219 ATP2A1/SERCA1 (L24) Antibody
- 9580 ATP2A2/SERCA2 (D51B11) Rabbit mAb
- 4388 ATP2A2/SERCA2 Antibody
- 5842 PKA C-α (D38C6) Rabbit mAb
- 4782 PKA C-α Antibody
- 5675 PKA RI-α (D54D9) Rabbit mAb
- 3927 PKA RI-α/β Antibody
- 9621 Phospho-(Ser/Thr) PKA Substrate Antibody
- 5661 Phospho-PKA C (Thr197) (D45D3) Rabbit mAb
- 7071 Phototope®-HRP Western Blot Detection System, Anti-rabbit IgG, HRP-linked Antibody
- 7074 Anti-rabbit IgG, HRP-linked Antibody
- 7720 Prestained Protein Marker, Broad Range (Premixed Format)
- 7727 Biotinylated Protein Ladder Detection Pack
- 7003 20X LumiGLO® Reagent and 20X Peroxide
- 9997 Tris Buffered Saline with Tween® 20 (TBST-10X)
- 9998 BSA
- 9999 Nonfat Dry Milk
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.