PTP1B (phospho-Tyr-152) Blocking Peptide
€155.00
In stock
SKU
ECM-PX2395
Background:
PTP1B is a nonreceptor type protein tyrosine phosphatase that has essential roles in insulin and leptin signaling, as well as important functions in growth factor and integrin signaling. The structure of PTP1B includes a conserved phosphatase domain, C-terminal hydrophobic residues for targeting to the cytoplasmic face of the endoplasmic reticulum, and proline-rich regions characteristic of SH3 domain binding motifs. PTP1B can interact with N-Cadherin and dephosphorylate β-catenin associated with cadherin complexes. PTP1B also interacts with Insulin and EGF receptors, and undergoes phosphorylation after receptor stimulation. Tyrosine phosphorylation at Tyr-66, Tyr-152, and Tyr-153 occurs after insulin receptor activation, and tyrosine phosphorylation of Tyr-152 may be required for interactions with N-Cadherin. In addition, Akt can phosphorylate Ser-50 and this phosphorylation can reduce PTP1B activity.
Sequence: Phospho-PTP1B (Tyr-152) synthetic peptide corresponds to amino acids surrounding Tyr-152 in human PTP1B. This sequence has significant homology to the conserved site in rat and mouse PTP1B, and has homology to conserved sites in TC-PTP and MPTP, but not other protein tyrosine phosphatase family members.
Specificity: This peptide is specifically recognized by PTP1B (Tyr-152) phospho-specific antibody (PP2391) in ELISA, and has been shown to block the reactivity of PP2391 in Western blot and is recommended for blocking 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.
PTP1B is a nonreceptor type protein tyrosine phosphatase that has essential roles in insulin and leptin signaling, as well as important functions in growth factor and integrin signaling. The structure of PTP1B includes a conserved phosphatase domain, C-terminal hydrophobic residues for targeting to the cytoplasmic face of the endoplasmic reticulum, and proline-rich regions characteristic of SH3 domain binding motifs. PTP1B can interact with N-Cadherin and dephosphorylate β-catenin associated with cadherin complexes. PTP1B also interacts with Insulin and EGF receptors, and undergoes phosphorylation after receptor stimulation. Tyrosine phosphorylation at Tyr-66, Tyr-152, and Tyr-153 occurs after insulin receptor activation, and tyrosine phosphorylation of Tyr-152 may be required for interactions with N-Cadherin. In addition, Akt can phosphorylate Ser-50 and this phosphorylation can reduce PTP1B activity.
Sequence: Phospho-PTP1B (Tyr-152) synthetic peptide corresponds to amino acids surrounding Tyr-152 in human PTP1B. This sequence has significant homology to the conserved site in rat and mouse PTP1B, and has homology to conserved sites in TC-PTP and MPTP, but not other protein tyrosine phosphatase family members.
Specificity: This peptide is specifically recognized by PTP1B (Tyr-152) phospho-specific antibody (PP2391) in ELISA, and has been shown to block the reactivity of PP2391 in Western blot and is recommended for blocking 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.
| Is Featured? | No |
|---|
Write Your Own Review