Technical Data
ATPase 2, Ca2+ Transporting, Sarcoplasmic Endoplasmic Reticulum (SERCA2)
ATP dependent calcium pumps are responsible, in part, for the maintenance of low cytoplasmic free calcium concentrations. The ATP pumps that reside in intracellular organelles are encoded by a family of structurally related enzymes, termed the sarcoplasmic or endoplasmic reticulum calcium (SERCA) ATPases. The SERCA1 gene is exclusively expressed in type II (fast) skeletal muscle. The SERCA2 gene is subject to tissue dependent processing which is responsible for the generation of SERCA2a muscle-specific form expressed in type I (slow) skeletal, cardiac and smooth muscle and the SERCA2b isoform expressed in all cell types. The SERCA3 gene is not as well characterized and is found in non-muscle cells.

Suitable for use in Immunocytochemistry, Immunohistochemistry and Western Blot. Other applications have not been tested.

Recommended Dilutions:
Immunohistochemistry (frozen sections): 1:500
Western Blot: 1:2500 Detects a band of ~110kD
Note: For detection of rat SERCA2 ATPase use A4000-93A.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20CBlue IceCanineMouse
Not determined
Purified canine cardiac sarcoplasmic reticulum.
Supplied as a liquid in PBS, 0.05% sodium azide.
Recognizes canine SERCA2a (sarcoplasmic/endoplasmic reticulum calcium ATPase 2a) and SERCA2b isoforms. Species crossreactivity: human, rat, porcine, bovine, rat. Does not crossreact with frog SERCA2 ATPase.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. A.O. Jorgensen, et al.; Cell Motil. Cytoskeleton 9, 164 (1988) 2. M.A. Movsesian, et al.; J. Mol. Cell. Cardiol. 22, 1477 (1990) 3. F.N. Briggs, et al.; FEBS Lett. 259, 269 (1990) 4. L. Plessers, et al.; J. Neurosci. 11, 650 (1991) 5. E. Molnar, et al.; Biochim. Biophys. Acta 1103, 281 (1992) 6. K.M. Mearow, et al.; Mol. Cell. Biochem. 121, 155 (1993) 7. C. Magnier, et al.; Biochem. J. 297, 343 (1994) 8. P. Hu, et al.; J. Biol. Chem. 270, 11619 (1995) 9. E. Poch, et al.; Am. J. Physiol. 275, C1449 (1998) 10. C.M. Misquitta, et al.; Biochem. J. 338, 167 (1999)11. C. Lacabaratz-Porret, et al.; Biochem. J. 350, 723 (2000) 12. M.R. Sepulveda, et al.; Eur. J. Neurosci. 19, 542 (2004) 13. I.L. Ennis, et al.; J. Clin. Invest. 109, 393 (2002)