protein

GDF-2/BMP-9 Protein, Human (P. pastoris, His)

HY-P700530

20 μg;50 μg

190;400 USD

GDF-2/BMP-9 Protein, Human (P. pastoris, His)

proteins

P. pastoris

20 μg;50 μg

190;400 USD

The BMP-9/GDF-2 protein is a potent inhibitor of angiogenesis that selectively signals through AVRL1 in endothelial cells. Its signaling pathway requires the TGF-β coreceptor endoglin/ENG to effectively activate SMAD1. GDF-2/BMP-9 Protein, Human (P. pastoris, His) is the recombinant human-derived GDF-2 protein, expressed by P. pastoris , with N-6*His labeled tag.

Human

BMP-9/GDF-2 Protein emerges as a potent circulating inhibitor of angiogenesis, specifically signaling through the type I activin receptor ACVRL1 while excluding other Alks. In endothelial cells, its signaling pathway involves the requirement for the TGF-beta coreceptor endoglin/ENG for efficient activation of SMAD1. Existing as a homodimer with disulfide-linked structures, BMP-9/GDF-2 is detected in extracellular fluid both as a mature homodimer and in complex with its propeptide. The protein establishes high-affinity interactions with ACVRL1, BMPR2, and ACVR2B, crucial for its signal transduction cascade. Furthermore, it forms complexes with ENG, either as a heterotetramer with a 2:2 stoichiometry or as a heteromeric complex with ENG and ACVRL1. Notably, it also interacts with the type I receptor ACVR1, contributing to the intricate regulatory network within the TGF-beta signaling pathway.

GDF-2; BMP-9; GDF2; BMP9

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.