Recombinant Human PSTPIP1 protein (His tag N-Terminus)
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Recombinant Human PSTPIP1 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 416 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
CD2BP1, PSTPIP1, Proline-serine-threonine phosphatase-interacting protein 1, PEST phosphatase-interacting protein 1, CD2-binding protein 1, H-PIP
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PSTPIP1 protein (His tag N-Terminus) (AB167828)
15% SDS-PAGE analysis of 3µg ab167828.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PSTPIP1 interacts with several proteins to regulate cellular processes including inflammation and cell movement. It is known to bind to PTP-PEST a protein tyrosine phosphatase which plays a role in cytoskeletal organization. PSTPIP1 is also found in complexes that can alter the actin cytoskeleton influencing cell adhesion and motility. This interaction impacts immune responses and signaling pathways in cells playing an important role in maintaining cellular integrity under various physiological conditions.
Pathways
PSTPIP1 contributes to the regulation of the actin cytoskeleton and inflammatory pathways. It participates in the signaling pathways that involve the Wiskott-Aldrich syndrome protein (WASP) which connects to actin polymerization processes. Additionally PSTPIP1 links with the proteins in the NF-kB pathway participating in the modulation of immune responses. This positioning in multiple pathways allows PSTPIP1 to influence cellular responses significantly.
Specifications
Form
Liquid
Additional notes
ab167828 was purified using conventional chromatography techniques.
General info
Function
Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell : APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils.
Post-translational modifications
Dephosphorylated on Tyr-345 by PTPN18, this event negatively regulates the association of PSTPIP1 with SH2 domain-containing proteins as tyrosine kinase. Phosphorylation of Tyr-345 is probably required for subsequent phosphorylation at other tyrosine residues. Phosphorylation is induced by activation of the EGFR and PDGFR in a ABL1 dependent manner. The phosphorylation regulates the interaction with WAS and with MEFV (By similarity).
Subcellular localisation
Cytoskeleton
Target data
Complementary Products
Product promise
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