Paxillin (phospho-Thr-538) Blocking Peptide
€155.00
In stock
SKU
ECM-PX4495
Background:
Paxillin, a focal adhesion protein, is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and SH3-/SH2-binding domains that participate in a variety of protein-protein interactions with kinases, GTPase-activating proteins, and cytoskeletal proteins. Phosphorylation of paxillin occurs at tyrosine, threonine, and serine sites. Serine and threonine phosphorylation of paxillin occur in response to growth-factor activation, PKC activators, and fibronectins. Phosphorylation of Ser-85, Ser-178, and Thr-538 may be important sites for regulating paxillin activity. Paxillin phosphorylation of Thr-538 occurs in response to TPA-activated PKCs in vitro, and this phosphorylation may contribute to dissolution of the actin cytoskeleton and redistribution of LFA-1 integrins in vivo.
Sequence: Phospho-Paxillin (Thr-538) synthetic peptide corresponding to amino acid residues around threonine 538 from human paxillin a. This sequence is highly conserved in rat and mouse paxillin and is also found in the other paxillin isoforms (b & g).
Specificity: The peptide is specifically recognized by anti-Paxillin (Thr-538) phospho-specific antibody (PP4491) in ELISA, and has been shown to block the reactivity of PP4491 during Western blot. In addition, the peptide is recommended for use in blocking PP4491 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.
Paxillin, a focal adhesion protein, is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and SH3-/SH2-binding domains that participate in a variety of protein-protein interactions with kinases, GTPase-activating proteins, and cytoskeletal proteins. Phosphorylation of paxillin occurs at tyrosine, threonine, and serine sites. Serine and threonine phosphorylation of paxillin occur in response to growth-factor activation, PKC activators, and fibronectins. Phosphorylation of Ser-85, Ser-178, and Thr-538 may be important sites for regulating paxillin activity. Paxillin phosphorylation of Thr-538 occurs in response to TPA-activated PKCs in vitro, and this phosphorylation may contribute to dissolution of the actin cytoskeleton and redistribution of LFA-1 integrins in vivo.
Sequence: Phospho-Paxillin (Thr-538) synthetic peptide corresponding to amino acid residues around threonine 538 from human paxillin a. This sequence is highly conserved in rat and mouse paxillin and is also found in the other paxillin isoforms (b & g).
Specificity: The peptide is specifically recognized by anti-Paxillin (Thr-538) phospho-specific antibody (PP4491) in ELISA, and has been shown to block the reactivity of PP4491 during Western blot. In addition, the peptide is recommended for use in blocking PP4491 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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