ARPIN Antibody / Actin-related protein complex inhibitor, 100 ug

ARPIN antibody detects Actin-related protein complex inhibitor (Arpin), a negative regulator of actin filament branching that modulates cell motility and migration. The UniProt recommended name is Actin-related protein complex inhibitor (ARPIN). This cytoplasmic protein inhibits the Arp2/3 complex, controlling actin polymerization dynamics essential for lamellipodia formation, directional movement, and membrane protrusion regulation.

Functionally, ARPIN antibody identifies a 220-amino-acid protein that binds directly to the Arp2/3 complex through its C-terminal acidic motif, competing with activating factors such as WASP and WAVE. By inhibiting Arp2/3-dependent actin nucleation, ARPIN reduces protrusive force at the cell leading edge, promoting turning behavior and directional persistence. The protein is involved in establishing cell polarity, controlling migration speed, and maintaining cytoskeletal balance between extension and contraction.

The ARPIN gene (also known as C15orf38) is located on chromosome 15q24.1 and is expressed in multiple tissues, particularly in epithelial cells, fibroblasts, and neurons. Its activity is tightly regulated by upstream signaling through Rac1 and PI3K pathways that coordinate motility and cell shape remodeling.

Pathologically, altered ARPIN expression affects wound healing, cancer cell migration, and metastasis. Downregulation enhances cell motility and invasion by releasing inhibition of Arp2/3, while overexpression restricts lamellipodia formation and limits tumor spread. ARPIN thus acts as a molecular brake on cytoskeletal dynamics and metastatic progression. Research using ARPIN antibody supports studies in cytoskeletal biology, cancer metastasis, and motility regulation.

ARPIN antibody is validated for western blotting, immunofluorescence, and immunohistochemistry to detect actin regulatory proteins. NSJ Bioreagents provides ARPIN antibody reagents optimized for studies in actin network modulation, cell migration, and intracellular signaling control.

Structurally, Actin-related protein complex inhibitor consists of an N-terminal acidic region, a coiled-coil central domain, and a conserved C-terminal WCA-like motif that mediates interaction with Arp2/3. This domain organization allows ARPIN to act as a direct inhibitor without requiring scaffolding cofactors. This antibody facilitates investigation of ARPIN's role in cytoskeletal remodeling and directional motility across diverse biological systems.