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SERCA2 ATPase monoclonal antibody (2A7-A1)

ALX-804-088-R100 100 µl 778.00 USD
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Replaces Prod. #: BML-SA209

Product Details

Alternative Name:Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Immunogen:Purified dog cardiac sarcoplasmic reticulum vesicles.
UniProt ID:O46674
Species reactivity:Human, Mouse, Rat
Dog, Guinea pig, Porcine, Rabbit
Specificity:Recognizes SERCA2a and SERCA2b isoforms identically.
Applications:Flow Cytometry, ICC, IHC (FS), IHC (PS), IP, WB
Recommended Dilutions/Conditions:Flow Cytometry (1µg per 106 cells)
Immunocytochemistry (1:250)
Immunohistochemistry (paraffin sections, 1µg/ml)
Immunohistochemistry(frozen sections, 1:100)
Western Blot (1:1,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Application Notes:Detects a band of ~110kDa by Western blot.
Formulation:Liquid. Ascites diluted in PBS containing 0.05% sodium azide.
Handling:Avoid freeze/thaw cycles.
Shipping:Blue Ice
Long Term Storage:-20°C
Scientific Background: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 comprised of a family of structurally related enzymes, termed the sarcoplasmic or endoplasmic reticulum calcium (SERCA) ATPases. The SERCA2 gene is subject to tissue dependent processing which is responsible for the generation of SERCA2a muscle-specific isoform 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.
Regulatory Status:RUO - Research Use Only

Product Literature References

A novel interaction mechanism accounting for different acylphosphatase effects on cardiac and fast twitch skeletal muscle sarcoplasmic reticulum calcium pumps: C. Nediani, et al.; FEBS Lett. 443, 308 (1999), Abstract;

General Literature References

Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum: L.R. Jones, et al.; J. Biol. Chem. 270, 30787 (1995), Abstract;
Ca(2+)-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium: M.A. Movsesian, et al.; Circulation 90, 653 (1994), Abstract;
Molecular and physiological alterations in murine ventricular dysfunction: H.A. Rockman, et al.; Proc. Natl. Acad. Sci. USA 91, 2694 (1994), Abstract;

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