PSTPIP1 (proline-serine-threonine phosphatase interacting protein 1) is a cytoskeleton-associated adaptor protein, which contains an F-BAR (bin-amphiphysin-Rvs) domain. It shares high homology to PSTPIP2 protein, and is composed of an N-terminal Fer-CIP4 homology (FCH) domain and a PEST-type phosphatase-binding domain in its coiled coil region. It also contains an SH3 domain in its C-terminal.
Synonyms: Anti-CD2-binding protein 1; Anti-H-PIP; Anti-PEST phosphatase-interacting protein 1; Anti-Proline-serine-threonine phosphatase-interacting protein 1
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: PSTPIP1 (proline-serine-threonine phosphatase interacting protein 1) is associated with the inflammatory disorder called PAPA syndrome, which is characterized by pyogenic sterile arthritis, pyoderma gangrenosum, and acne, hence the name. This protein controls invasive macrophage migration and mediates the transformation from podosomes to filopodia-like protrusions. This protein forms a component of the leukocyte uropod, where it mediates endocytosis and cell migration.
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