protein

Semaphorin-5A/SEMA5A Protein, Human (HEK293, His)

HY-P70496

10 μg;50 μg

125;320 USD

Semaphorin-5A/SEMA5A Protein, Human (HEK293, His)

proteins

HEK293

10 μg;50 μg

125;320 USD

Semaphorin-5A/SEMA5A proteins act as bifunctional axon guidance signals, exerting attraction via heparan sulfate proteoglycans and inhibitory effects via chondroitin sulfate proteoglycans. As a ligand for the PLXNB3 receptor, SEMA5A disrupts glioma cell migration and invasion and induces cell collapse. Semaphorin-5A/SEMA5A Protein, Human (HEK293, His) is the recombinant human-derived Semaphorin-5A/SEMA5A protein, expressed by HEK293 , with C-6*His labeled tag. The total length of Semaphorin-5A/SEMA5A Protein, Human (HEK293, His) is 743 a.a., with molecular weight of ~100.0 kDa.

Human

Semaphorin-5A/SEMA5A Protein functions as a bifunctional axonal guidance cue regulated by sulfated proteoglycans, exhibiting attractive effects through interactions with heparan sulfate proteoglycans (HSPGs), and inhibitory effects dependent on interactions with chondroitin sulfate proteoglycans (CSPGs). As a ligand for receptor PLXNB3, SEMA5A plays a crucial role in glioma cells, where its stimulation of PLXNB3 leads to the disassembly of F-actin stress fibers, disruption of focal adhesions, cellular collapse, and the inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. Furthermore, SEMA5A may promote angiogenesis by enhancing endothelial cell proliferation and migration while inhibiting apoptosis. The binding of SEMA5A to PLXNB3 underscores its involvement in diverse cellular processes, providing valuable insights into its potential roles in both normal development and pathological conditions, particularly in the context of axon guidance, cell migration, and angiogenesis.

Semaphorin-5A; Semaphorin-F; Sema F; SEMA5A; SEMAF

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.