Actin (N-terminal Region) Blocking Peptide
€155.00
In stock
SKU
ECM-AX1655
Background:
Actin is a major cytoskeletal protein involved in diverse cellular functions including cell motility, adhesion, and morphology. Six different actin isoforms have been identified in vertebrates. There are four α isoforms: skeletal, cardiac, and two smooth muscle (enteric and aortic) actins, along with two cytoplasmic actins (β and γ). Actin exists in two principal forms, globular, monomeric (G) actin, and filamentous polymeric (F) actin. The assembly and disassembly of actin filaments, and also their organisation into functional networks, is regulated by a variety of actin-binding proteins (ABPs). Phosphorylation may also be important for regulating actin assembly and interaction with ABPs. In Dictyostelium, phosphorylation of Tyr-53 occurs in response to cell stress and this phosphorylation may alter actin polymerizaiton. In B cells, SHP-1 tyrosine dephosphorylation of actin leads to actin filament depolymerization following BCR stimulation.
Sequence: Actin synthetic peptide (coupled to KLH) corresponding to amino acid residues in the N-terminal region of human β actin. This sequence is identical to similar regions in all four α actins, as well as in g actin, and is well conserved in actins from most eukaryotic species.
Specificity: The peptide is specifically recognized by actin (N-terminal Region) antibody (AP1651) in ELISA, and has been shown to block the reactivity of AP1651 in Western blot and 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.
Actin is a major cytoskeletal protein involved in diverse cellular functions including cell motility, adhesion, and morphology. Six different actin isoforms have been identified in vertebrates. There are four α isoforms: skeletal, cardiac, and two smooth muscle (enteric and aortic) actins, along with two cytoplasmic actins (β and γ). Actin exists in two principal forms, globular, monomeric (G) actin, and filamentous polymeric (F) actin. The assembly and disassembly of actin filaments, and also their organisation into functional networks, is regulated by a variety of actin-binding proteins (ABPs). Phosphorylation may also be important for regulating actin assembly and interaction with ABPs. In Dictyostelium, phosphorylation of Tyr-53 occurs in response to cell stress and this phosphorylation may alter actin polymerizaiton. In B cells, SHP-1 tyrosine dephosphorylation of actin leads to actin filament depolymerization following BCR stimulation.
Sequence: Actin synthetic peptide (coupled to KLH) corresponding to amino acid residues in the N-terminal region of human β actin. This sequence is identical to similar regions in all four α actins, as well as in g actin, and is well conserved in actins from most eukaryotic species.
Specificity: The peptide is specifically recognized by actin (N-terminal Region) antibody (AP1651) in ELISA, and has been shown to block the reactivity of AP1651 in Western blot and 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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