Arp2 (phospho-Thr-237/Thr-238) Blocking Peptide
€155.00
In stock
SKU
ECM-AX3875
Background:
Cellular morphology, adhesion, and motility occur through dynamic reorganization of actin-based superstructures. Actin-binding proteins are critical for regulating actin polymerization and superstructure formation. The Arp2/3 complex is an actin polymerization-inducing complex that includes Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. Several nucleation promoting factors, such as WASP and coronin, regulate the activity of the Arp2/3 complex. In addition, the Arp2/3 complex may be regulated by phosphorylation of specific subunits in the complex. Arp2 has two phosphosites, Thr-237 and Thr-238, that are evolutionarily conserved, and are phosphorylated along with Tyr-202 in response to growth factor stimulation. These phosphorylation events may regulate binding to the pointed end of actin filaments, and alanine substitutions of these Arp2 phosphosites inhibits membrane protrusions. Thus, phosphorylation may be another mode of Arp2/3 complex regulation in addition to the activity of nucleation-promoting factors.
Sequence: Phospho-Arp2 (Thr-237/Thr-238) synthetic peptide corresponding to amino acid residues surrounding threonine 237 and threonine 238 in human Arp2. This peptide sequence is highly conserved in rat, mouse, chicken, and fish Arp2 proteins.
Specificity: The peptide is specifically recognized by Arp2 (Thr-237/Thr-238) phospho-specific antibody (AP3871) in ELISA, and has been shown to block the reactivity of AP3871 in Western blot. In addition, the peptide is recommended for use in blocking AP3871 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.
Cellular morphology, adhesion, and motility occur through dynamic reorganization of actin-based superstructures. Actin-binding proteins are critical for regulating actin polymerization and superstructure formation. The Arp2/3 complex is an actin polymerization-inducing complex that includes Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. Several nucleation promoting factors, such as WASP and coronin, regulate the activity of the Arp2/3 complex. In addition, the Arp2/3 complex may be regulated by phosphorylation of specific subunits in the complex. Arp2 has two phosphosites, Thr-237 and Thr-238, that are evolutionarily conserved, and are phosphorylated along with Tyr-202 in response to growth factor stimulation. These phosphorylation events may regulate binding to the pointed end of actin filaments, and alanine substitutions of these Arp2 phosphosites inhibits membrane protrusions. Thus, phosphorylation may be another mode of Arp2/3 complex regulation in addition to the activity of nucleation-promoting factors.
Sequence: Phospho-Arp2 (Thr-237/Thr-238) synthetic peptide corresponding to amino acid residues surrounding threonine 237 and threonine 238 in human Arp2. This peptide sequence is highly conserved in rat, mouse, chicken, and fish Arp2 proteins.
Specificity: The peptide is specifically recognized by Arp2 (Thr-237/Thr-238) phospho-specific antibody (AP3871) in ELISA, and has been shown to block the reactivity of AP3871 in Western blot. In addition, the peptide is recommended for use in blocking AP3871 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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