|Application ||WB, FC, E|
|Other Accession||P97814, NP_003969.2|
|Calculated MW||47591 Da|
|Antigen Region||89-118 aa|
|Other Names||Proline-serine-threonine phosphatase-interacting protein 1, PEST phosphatase-interacting protein 1, CD2-binding protein 1, H-PIP, PSTPIP1, CD2BP1|
|Target/Specificity||This PSTPIP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 89-118 amino acids from the N-terminal region of human PSTPIP1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PSTPIP1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|Cellular Location||Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, uropodium. Cytoplasm, perinuclear region. Cleavage furrow. Note=During interphase, colocalizes with F- actin in the cortical cytoskeleton, lamellipodia, and stress fibers. In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow. Colocalized with WAS to filamentous structures within the cytoplasm. Colocalized with PTPN12 in the cytoplasm and the perinuclear region. Colocalized with CD2AP and WAS in the actin cytoskeleton. Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (By similarity). In monocytes, forms a branched filamentous network in the cytoplasm. In migrating neutrophils, localizes most strongly to the trailing edge of the uropod where it colocalizes with PIP5K1C. In transfected cells, forms relatively straight filaments radiating out from the nucleus. Colocalizes with MEFV, particularly at the branch point of filaments. Filament formation requires an intact tubulin cytoskeleton.|
|Tissue Location||Highly expressed in the peripheral blood leukocytes, granulocytes and monocytes, namely in T-cells and natural killer cells, and in spleen. Weakly expressed in the thymus, small intestine, lung and placenta|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene binds to the cytoplasmic tail of CD2, an effector of T cell activation and adhesion, negatively affecting CD2-triggered T cell activation. The encoded protein appears to be a scaffold protein and a regulator of the actin cytoskeleton. It has also been shown to bind ABL1, PTPN18, WAS, CD2AP, and PTPN12. Mutations in this gene are a cause of PAPA syndrome.
Andre, M.F., et al. Dig. Dis. Sci. 55(6):1681-1688(2010)
Rose, J. Phd, et al. Mol. Med. (2010) In press :
Hong, J.B., et al. J. Am. Acad. Dermatol. 61(3):533-535(2009)
Voss, M., et al. BMC Immunol. 10, 53 (2009) :
Waite, A.L., et al. PLoS ONE 4 (7), E6147 (2009) :
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