GARP (Mutated)&Latent TGF Beta Complex Protein, Human (HEK293, His-Avi)

LRRC32 is a key regulator of TGF-β activation and maintains TGFB1, TGFB2, and TGFB3 in the latent state during extracellular storage by binding to latency-associated peptide (LAP). LRRC32 competes with LTBP1 for LAP binding and effectively regulates integrin-dependent TGF-β activation. GARP (Mutated) &Latent TGF Beta Complex Protein, Human (HEK293, His-Avi) is a recombinant protein dimer complex containing human-derived GARP, expressed by HEK293 , with C-Avi, C-His labeled tag. GARP (Mutated) &Latent TGF Beta Complex Protein, Human (HEK293, His-Avi), has molecular weight of 75-80 kDa.

LRRC32, a crucial regulator of transforming growth factor beta (TGFB1, TGFB2, and TGFB3), plays a pivotal role in controlling TGF-beta activation by maintaining it in a latent state during extracellular storage. Specifically associating with the Latency-associated peptide (LAP), the regulatory chain of TGF-beta, LRRC32 exerts its regulatory influence on integrin-dependent TGF-beta activation. Notably, LRRC32 competes effectively with LTBP1 for LAP binding, further modulating TGF-beta activation. Its significance extends to the regulation of TGF-beta-1 (TGFB1) activation on the surface of activated regulatory T-cells (Tregs). Moreover, LRRC32's involvement is essential for epithelial fusion during palate development, where it regulates the activation of TGF-beta-3 (TGFB3). Interacting directly with TGFB1, TGFB2, and TGFB3, LRRC32's association with LAP regulates the activation of TGF-beta-1 and TGF-beta-3, highlighting its intricate role in fine-tuning TGF-beta signaling. Additionally, LRRC32 interacts with LAPTM4B, contributing to the reduction of TGFB1 production in regulatory T-cells.

Human

HEK293

C-Avi;C-His

Q14392 (H20-L628, Y137H, S138G, G139N)&P01137 (L30

2615  [NCBI]&7040  [NCBI]

75-80 kDa

Greater than 95% as determined by Tris-Bis PAGE.

<1 EU/μg, determined by LAL method.