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SERCA2 Phospho-Ser38 Epitope Peptide

Catalogue No.: P010-25           Unit Size: 50 nmoles; sufficient for 50 mls of western blot reagent at 1 μM

Price: £68 / €114 / US$143        Place an order

Background: SERCA2 belongs to the P-type family of ATPases (Xu et al., 1993; Toyofuku et al., 1994; Hawkins et al., 1994; Osada et al., 1998; Netticadan et al., 1999; Netticadan et al., 2000). Controversy still surrounds the phosphorylation status of Ser-38 and its physiological implication. Some groups have reported that Ser-38 of SERCA2 is phosphorylated by CaMKII, which apparently leads to a substantial increase in ATPase activity (Xu et al., 1993; Hawkins et al., 1994). However, the control of Ca²⁺-pump function by direct phosphorylation has not been observed by all investigators (Odermatt et al., 1996; Reddy et al., 1996; Rodriguez et al., 2004). This antibody, described by Rodriguez et al. (2004), may help to resolve the controversy.

Description: Synthetic competing epitope peptide containing amino acids surrounding the phosphorylated serine residue at position 38 of SERCA2.

Peptide Sequence:   

GMBS-GG- K₃₁LKERWGS(PO3H2)NEL₄₁

M. W. = 1718.1 Da. Sequence in bold = native epitope sequence.

Specificity: Addition of the peptide to the primary antibody incubation at a 1 μM final concentration is sufficient to prevent the recognition of the anti-SERCA2 phospho-Ser38 antibody to its target epitope (see Quality Control Certificate for the anti-SERCA2 phospho-Ser38 antibody).

Quality Control Certificate of Analysis                Link to larger images

Related Products: Anti-SERCA2 phospho-Ser38 antibody (A010-25). SERCA2 phospho-Ser38 positive control (C010-25).

Background References:                                                          

• Hawkins, C., Xu, A., and Narayanan, N. (1994): J Biol Chem 269, 31198-206.                                                                           

• Netticadan, T., Temsah, R., Osada, M., and Dhalla, N. S. (1999): Am J Physiol 277, C384-91.                                           

• Netticadan, T., Temsah, R. M., Kawabata, K., and Dhalla, N. S. (2000): Circ Res 86, 596-605.                                                

• Odermatt, A., Kurzydlowski, K., and MacLennan, D. H. (1996): J Biol Chem 271, 14206-13.                                                                      

• Osada, M., Netticadan, T., Tamura, K., and Dhalla, N. S. (1998): Am J Physiol 274, H2025-34.                                         

• Reddy, L. G., Jones, L. R., Pace, R. C., and Stokes, D. L. (1996): J Biol Chem 271, 14964-70.                                            

• Rodriguez, P., Jackson, W. A., and Colyer, J. (2004): J Biol Chem 279, 17111-9.                                                                   

• Toyofuku, T., Curotto Kurzydlowski, K., Narayanan, N., and MacLennan, D. H. (1994): J Biol Chem 269, 26492-6.                

• Xu, A., Hawkins, C., and Narayanan, N. (1993): J Biol Chem 268, 8394-7.

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Last modified: January 04, 2007