Recombinant Human PSTPIP1 protein is a Human Full Length protein, in the 1 to 416 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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.
CD2BP1, PSTPIP1, Proline-serine-threonine phosphatase-interacting protein 1, PEST phosphatase-interacting protein 1, CD2-binding protein 1, H-PIP
Recombinant Human PSTPIP1 protein is a Human Full Length protein, in the 1 to 416 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab167828 was purified using conventional chromatography techniques.
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.
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).
PSTPIP1 also known as Proline-Serine-Threonine Phosphatase Interacting Protein 1 is a cytoplasmic adaptor protein with a molecular weight of approximately 47 kDa. It mainly functions in the regulation of the actin cytoskeleton. This protein contains an F-BAR domain and a SH3 domain allowing it to bind membranes and other proteins affecting cytoskeletal dynamics. PSTPIP1 is expressed in various tissues including hematopoietic cells where it plays significant roles in immune cell function.
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.
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.
PSTPIP1 mutations and dysregulation have been linked to conditions such as pyogenic arthritis pyoderma gangrenosum and acne (PAPA) syndrome. In these diseases PSTPIP1 interacts with proteins such as PTP-PEST and pyrin which are critical in controlling inflammation. Abnormal interactions or mutations in PSTPIP1 can lead to hyperactivation of inflammation contributing to the symptoms observed in these disorders highlighting its important role in immune regulation and pathology.
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15% SDS-PAGE analysis of 3µg ab167828.
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