protein

GARP&Latent TGF Beta-1 Complex Protein, Human (HEK293, His, Strep)

HY-P72636

10 μg;50 μg

160;450 USD

GARP&Latent TGF Beta-1 Complex Protein, Human (HEK293, His, Strep)

proteins

HEK293

10 μg;50 μg

160;450 USD

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&Latent TGF Beta-1 Complex Protein, Human (HEK293, His, Strep) is a recombinant protein dimer complex containing human-derived GARP&Latent TGF Beta-1 Complex protein, expressed by HEK293 , with N-6*His, C-3*Strep labeled tag. GARP&Latent TGF Beta-1 Complex Protein, Human (HEK293, His, Strep), has molecular weight of 10-14 & 35-50 & 85-95 kDa, respectively.

Human

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.

GARP&Latent TGF Beta-1 Complex Protein

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

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.