Novel HIF2A mutations disrupt oxygen sensing, leading to polycythemia, paragangliomas, and somatostatinomas Blood, Mar 2013; 121: 2563 - 2566.
[anti-HA]
Regulation of the PI3-K/Akt Survival Pathway in the Rat Endometrium Biol Reprod, Mar 2013; 88: 79.
[Akt3]
RNA elements directing in vivo assembly of the 7SK/MePCE/Larp7 transcriptional regulatory snRNP Nucleic Acids Res., Mar 2013; 10.1093/nar/gkt159.
[LA]
Ruxolitinib as potential targeted therapy for patients with JAK2 rearrangements Haematologica, Mar 2013; 98: 404 - 408.
[JAK2]
A phospho specific peptide corresponding to residues surrounding serine 8 of human Parvin was used as an immunogen. This antibody detects Actopaxin phosphorlyated on serine 8.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Actopaxin (also named Parvin, Parva) is a member of the alpha actinin superfamily containing a single alpha-actinin-like actin-binding domain. The Parvin family plays a role in cell adhesion and cytoskeleton organization. Analysis of Actopaxin and its para- and orthologues suggest, that the parvins represent a new family of alpha-actinin-related proteins that mediate cell-matrix adhesion (1). Actopaxin as a widely expressed protein that binds directly to both F-actin and paxillin LD1 and LD4 motifs. It exhibits robust focal adhesion localization in several cultured cell types but is not found along the length of the associated actin-rich stress fibers. Actopaxin colocalizes with paxillin to rudimentary focal complexes at the leading edge of migrating cells. Results suggest an important role for actopaxin in integrin-dependent remodeling of the actin cytoskeleton during cell motility and cell adhesion (2).
Related Pathway
Focal Adhesion
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