αII-Spectrin (a.a. 1171-1176) Blocking Peptide
€155.00
In stock
SKU
ECM-SX5605
Background:
Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, α and β, which intertwine to form heterodimers that can self associate into elongated tetramers. α-spectrin I and β-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectrin I and II with β-spectrin I to V. The structure of spectrins includes a succession of triple-helical repeats along with various domains, such as SH3 domain, EF hands, PH domains, and binding domains for ankyrin, actin, band 4.1, and calmodulin. α-spectrin II is a widely expressed non-erythroid spectrin that contains an SH3 domain, a calmodulin binding site, and two cleavage sites, one at Tyr-1176 for calpains and one at Asp-1185 for caspase-3. α-spectrin II and β-spectrin II, like many other spectrins, can form heterodimers that can self associate into tetramers, as well as interact with Band 4.1, F-actin, and other proteins near the plasma membrane.
Background References
Robert-Lewis, J.M. et al. (1994) J Neurosci. 14(6):3934.
Manya, H. et al. (2002) J Biol Chem. 277(38):35503.
Higuchi, M. et al. (2005) J Biol Chem. 280:15229.
Sequence: A synthetic peptide corresponding to amino acid residues 1171 to 1176 in human αII-spectrin. This sequence has high homology with similar regions in rat and mouse αII-spectrin, but is not found in other spectrin family members.
Specificity: The peptide is specifically recognized by αII-Spectrin (a.a. 1171-1176), cleavage-specific antibody (SP5601) in ELISA, and has been shown to block the reactivity of SP5601 in Western blot. In addition, the peptide is recommended for use in blocking SP5601 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, α and β, which intertwine to form heterodimers that can self associate into elongated tetramers. α-spectrin I and β-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectrin I and II with β-spectrin I to V. The structure of spectrins includes a succession of triple-helical repeats along with various domains, such as SH3 domain, EF hands, PH domains, and binding domains for ankyrin, actin, band 4.1, and calmodulin. α-spectrin II is a widely expressed non-erythroid spectrin that contains an SH3 domain, a calmodulin binding site, and two cleavage sites, one at Tyr-1176 for calpains and one at Asp-1185 for caspase-3. α-spectrin II and β-spectrin II, like many other spectrins, can form heterodimers that can self associate into tetramers, as well as interact with Band 4.1, F-actin, and other proteins near the plasma membrane.
Background References
Robert-Lewis, J.M. et al. (1994) J Neurosci. 14(6):3934.
Manya, H. et al. (2002) J Biol Chem. 277(38):35503.
Higuchi, M. et al. (2005) J Biol Chem. 280:15229.
Sequence: A synthetic peptide corresponding to amino acid residues 1171 to 1176 in human αII-spectrin. This sequence has high homology with similar regions in rat and mouse αII-spectrin, but is not found in other spectrin family members.
Specificity: The peptide is specifically recognized by αII-Spectrin (a.a. 1171-1176), cleavage-specific antibody (SP5601) in ELISA, and has been shown to block the reactivity of SP5601 in Western blot. In addition, the peptide is recommended for use in blocking SP5601 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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