*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
rat brain, mouse brain, NIH3T3
0.01M PBS pH7.4, 15 mM sodium azide
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Batch dependent (Please refer to the vial label for the specific concentration.)
synthetic peptide located near the C-terminus of mouse ASAP1 (amino acids 962-978) conjugated to KLH.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
ArfGAP with SH3 domain, ankyrin repeat and PH domain1 , AV239055 , DEF-1 , Ddef1 , PAP , mKIAA1249 , s19
ADP-ribosylation factors (ARFs) family of GTP binding proteins are involved in the regulation of membrane trafficking and actin cytoskeleton. ASAP1 (ARF GAP containing SH3, ANK repeat and PH domains 1, also known as DEF1 or centaurin beta 4) is a 130 kDa, ADP ribosylation factor GTPase activating protein (ARFGAP). ARFs require ARF-GAPs that stimulate their GTPase activity. ASAP1 belongs to a family of related ARF-GAP proteins, consisting of PAP/DEF2, ACAP1, ACAP2, GIT1/CAT1/APP1, and GIT2/CAT2/PKL, which are involved in the regulation of the actin cytoskeleton and cell migration. ASAP1 binds ARF1 and ARF5, with only modest activity toward ARF6. It also binds to other known regulators of actin cytoskeleton, such as tyrosine kinase Src, Crk, FAK and phosphatidylinositol-4,5-bisphosphate (PIP2). ASAP1 is phosphorylated on tyrosine residues in cells expressing activated Src.ASAP1a and ASAP1b are two variants formed by alternative splicing of the ASAP1 gene. ASAP1 localizes to focal adhesions and cycles with focal adhesion proteins when cells are stimulated to move. Overexpression of ASAP1 alters the morphology of focal adhesions, blocks cell spreading and formation of dorsal ruffles, and prevents the efficient organization of paxillin and FAK in focal adhesions. On the other hand, a mutation disrupting GAP activity of ASAP1 or overexpression of a truncated variant of ASAP1 that fails to bind FAK has a reduced effect on inhibition of cell spreading. By directly interacting with both ARFs and focal adhesion proteins such as paxillin and FAK, ASAP1 plays an important role in the regulation of focal adhesion assembly and cytoskeletal remodeling.