WebPhosphorylation of Y542 creates an interaction in the N-terminal SH2 domain and appears to relieve basal inhibition of the PTP, while phosphorylation at Y580 creates an interaction at the C-terminal that stimulates PTP activity. The L99-921 monoclonal antibody recognizes the phosphorylated Y542 of SHP2 (PTP2C isoform 2). WebThe L99-921 monoclonal antibody recognizes the phosphorylated Y542 of SHP2 (PTP2C isoform 2). The homologous phosphorylation site in the PTP2Ci splice variant (isoform 1) is Y546. The specificity of this antibody was validated by confirming, using western blot analysis, that RNA-mediated interference (RNAi) of the specific protein was able to ...
Role of the Tyrosine Phosphatase SHP-2 in Mediating ... - PubMed
WebSep 3, 2009 · Total cellular protein extracts were then subjected to Western blotting for P-SHP2 Y542 and Y580, total SHP2, and tubulin. Close modal We also compared the effects of M-CSF or G-CSF on the STAT1, STAT3, and STAT5 transcription factors or SHP2, a tyrosine phosphatase that contributes to ERK activation 26 ( Figure 2 C top panel lanes 1 … WebJan 2, 2024 · In contrast, p(Y542)SHP2 was virtually undetectable in certain BRAF(V600E) cells, in which RAS was feedback-activated independent of SHP2 (“SHP2-negative”) (Figure 4 C). These findings raised the possibility that a lack of SHP2 phosphorylation may help predict independence on SHP2 for feedback-induced RAS activation and thus tumor ... react native log error
Elaiophylin triggers paraptosis and preferentially kills ovarian …
WebRabbit Phospho-SHP2-Y542 Rabbit pAb (AP0267), validaed in WB,, IHC and tested in Human,, Mouse,, Rat. 100% Guaranteed. ABclonal provides trial size antibody samples … WebOct 20, 2024 · SHP2 converts the inactive form of KRAS into the activated form. Cancer cells may adapt to KRAS inhibition by increasing SHP2 activity, resulting in increased … WebEffective activity and synaptic content of tyrosine phosphatase SHP2 are required for AMPA receptor trafficking during LTP. However, the role of SHP2 in LTD has not been fully … react native loading skeleton