- Peptide (C)TPDQVKRHLEKYG, corresponding to amino acid residues 25-37 of rat SERCA1 (Accession Q64578). Cytoplasmic, N-terminus.
- Western blot analysis of mouse C2C12 myoblast cell line lysate (lanes 1 and 3) and rat skeletal muscle membranes (lanes 2 and 4):1,2. Anti-SERCA1 Antibody (#ACP-011), (1:200).
3,4. Anti-SERCA1 Antibody, preincubated with SERCA1 Blocking Peptide (#BLP-CP011).
- Expression of SERCA1 in rat skeletal muscleImmunohistochemical staining of rat skeletal muscle paraffin-embedded sections using Anti-SERCA1 Antibody (#ACP-011), followed by goat anti-rabbit-AlexaFluor-594 secondary antibody. A. SERCA1 labeling appears in the muscle fibers, in a pattern that could indicate the location of the sarcoplasmic reticulum. The endomysium, surrounding muscle fibers, is not stained. B. Nuclear staining using DAPI as the counterstain. C. Merged image of A and B.
- Expression of SERCA1 in mouse C2C12 myoblast cell lineImmunocytochemical staining of fixed and permeabilized C2C12 cells. A. Cells were stained with Anti-SERCA1 Antibody (#ACP-011), (1:400), followed by goat anti-rabbit-AlexaFluor-594 secondary antibody (red). B. Live image of the cells stained in A. C. Merge image of A and B and visualization of cell nuclei using Hoechst 33342 (blue).
Three Ca2+ ATPases have been described in mammalian cells. They are located in the plasma membrane, endoplasmic reticulum or the Golgi apparatus. SERCA pumps are located in both the endoplasmic reticulum and in the Golgi membranes. They are known to transport two Ca2+ molecules per hydrolysis of one ATP1. Their structure includes ten transmembrane domains and their main role is to remove cytoplasmic Ca2+ ions in order to promote muscle relaxation1.
In mammals three genes encode three SERCA pumps. Each transcript undergoes tissue-dependent alternative splicing. SERCA1a and 1b are expressed in adult and neonatal skeletal muscle respectively. SERCA2a is also expressed in skeletal muscle, while SERCA2b is ubiquitously expressed. SERCA3 is expressed in a limited number of non-muscle cells2. Although all SERCAs are regulated, SERCA2b undergoes extensive regulation at the protein level, such as protein-protein interaction, phosphorylation and glycosylation1.
The expression of SERCA1 in mice is essential3 whereas in human its absence is tolerated but is the cause of Brody myopathy4. Malfunction of SERCAs is also observed in heart disease and different forms of cancer1.
Species reactivity key:
Multiplex staining of SERCA1 and TRPV2 in mouse heart.Immunohistochemical staining of mouse heart immersion-fixed, free floating frozen sections, using rabbit Anti-SERCA1 Antibody (#ACP-011) (1:200) and Guinea pig Anti-TRPV2 (VRL1) (extracellular) Antibody (#AGP-033), (1:200). A. SERCA1 staining (green) appears in T tubules (arrows). B. TRPV2 staining (red) in same section is detected in intercalated discs (diagonal arrows) and T tubules (horizontal arrow). C. Merge of panels A and B demonstrates co-localization of SERCA1 and TRPV2. Nuclei are stained using DAPI (blue).
Anti-SERCA1 Antibody (#ACP-011) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot, immunohistochemistry, and immunocytochemistry applications. It has been designed to recognize SERCA1 from rat, mouse, and human samples.
- Mouse DRG sections (1:100).
Rouwette, T. et al. (2016) Mol. Cell. Proteomics 15, 2152.