This recombinant human ANGPT2 protein represents the biologically active form (amino acids 19-496) of human angiopoietin-2, produced in mammalian cells with C-terminal 10×His tagging. The recombinant ANGPT2 protein demonstrates exceptional purity (>90% by both SDS-PAGE and SEC-HPLC) and meets stringent endotoxin specifications (<1.0 EU/μg, LAL method), ensuring research-grade quality for vascular biology studies.
The ANGPT2 protein exhibits potent biological activity, showing high-affinity binding to anti-ANGPT2 antibody(CSB-RA001707MA01HU) in ELISA (EC50: 0.6666-0.8876 ng/mL at 2 μg/mL immobilization). The mammalian expression system guarantees proper protein folding and post-translational modifications essential for maintaining ANGPT2's native structural and functional characteristics.
Presented as lyophilized powder, this recombinant ANGPT2 protein offers enhanced stability and convenient reconstitution properties. The C-terminal 10×His tag enables efficient purification while preserving biological activity. This recombinant ANGPT2 is particularly valuable for angiogenesis research and vascular development studies, tumor microenvironment investigations, vascular permeability regulation studies, and in vitro and in vivo models of pathological angiogenesis.
ANGPT2 is a member of the angiopoietin family of growth factors that plays a crucial role in cardiovascular biology and pathology. ANGPT2 acts as a natural antagonist to the Tie2 receptor and participates in the destabilization of existing vasculature and facilitates neovascularization [1-3]. This antagonistic role is particularly pronounced under conditions of inflammation or tissue injury, where ANGPT2 levels increase to help initiate the repair processes through enhanced endothelial permeability and leukocyte recruitment [4].
The interplay between ANGPT2 and ANGPT1 is essential for maintaining vascular homeostasis. Under normal physiological conditions, ANGPT1 exerts its stabilizing effects on the endothelium through Tie2 receptor activation, whereas elevated levels of ANGPT2 can lead to a shift in this balance, resulting in increased endothelial cell dropout and a compromised vascular barrier [3]. This functional duality of ANGPT2 is critical in various pathologies, including cancer, where high levels of ANGPT2 correlate with tumor aggressiveness and poor patient outcomes due to enhanced tumor vascularization [5][6].
Research has indicated the presence of ANGPT2 not only in the systemic circulation but also locally in tissues such as the ovarian follicle, where it plays a significant role in regulating angiogenesis during the ovarian cycle [7]. Furthermore, ANGPT2 has been implicated in several diseases characterized by chronic inflammation, such as obesity and rheumatoid arthritis, suggesting its broader role in the pathology of conditions beyond classical angiogenesis [8][9].
Recent therapeutic strategies have emerged targeting ANGPT2 in cancer treatment, utilizing inhibitors to block its action and potentially curb tumor growth and metastasis [6]. Additionally, while ANGPT2 is often upregulated in solid tumors, its levels can serve as a prognostic biomarker in various cancers, underpinning its relevance in tumor biology and clinical outcomes [10]. Overall, ANGPT2 represents a critical factor in both physiological and pathological angiogenesis, with significant implications for understanding vascular biology and developing targeted therapies.
References:
[1] H. Chang, B. WANG, P. KUAN, & K. Shyu. Cyclical mechanical stretch enhances angiopoietin-2 and tie2 receptor expression in cultured human umbilical vein endothelial cells. Clinical Science, vol. 104, no. 4, p. 421-428, 2003. https://doi.org/10.1042/cs1040421
[2] D. Chen, K. Li, et al., Inhibition of angiopoietin-2 production by myofibrocytes inhibits neointimal hyperplasia after endoluminal injury in mice. Frontiers in Immunology, vol. 9, 2018. https://doi.org/10.3389/fimmu.2018.01517
[3] K. Rathnakumar, S. Savant, et al. Angiopoietin‐2 mediates thrombin‐induced monocyte adhesion and endothelial permeability. Journal of Thrombosis and Haemostasis, vol. 14, no. 8, p. 1655-1667, 2016. https://doi.org/10.1111/jth.13376
[4] S. Post, W. Peeters, et al. Balance between angiopoietin-1 and angiopoietin-2 is in favor of angiopoietin-2 in atherosclerotic plaques with high microvessel density. Journal of Vascular Research, vol. 45, no. 3, p. 244-250, 2008. https://doi.org/10.1159/000112939
[5] C. Sfiligoi, A. Luca, et al. Angiopoietin‐2 expression in breast cancer correlates with lymph node invasion and short survival. International Journal of Cancer, vol. 103, no. 4, p. 466-474, 2002. https://doi.org/10.1002/ijc.10851
[6] D. Hyman, N. Rizvi, et al. Phase i study of medi3617, a selective angiopoietin-2 inhibitor alone and combined with carboplatin/paclitaxel, paclitaxel, or bevacizumab for advanced solid tumors. Clinical Cancer Research, vol. 24, no. 12, p. 2749-2757, 2018. https://doi.org/10.1158/1078-0432.ccr-17-1775
[7] R. Tal, D. Seifer, R. Grazi, & H. Malter. Angiopoietin-1 and angiopoietin-2 are altered in polycystic ovarian syndrome (pcos) during controlled ovarian stimulation. Vascular Cell, vol. 5, no. 1, p. 18, 2013. https://doi.org/10.1186/2045-824x-5-18
[8] T. Okada, H. Tsukano, et al. Synoviocyte-derived angiopoietin-like protein 2 contributes to synovial chronic inflammation in rheumatoid arthritis. American Journal of Pathology, vol. 176, no. 5, p. 2309-2319, 2010. https://doi.org/10.2353/ajpath.2010.090865
[9] M. Tabata, T. Kadomatsu, et al. Angiopoietin-like protein 2 promotes chronic adipose tissue inflammation and obesity-related systemic insulin resistance. Cell Metabolism, vol. 10, no. 3, p. 178-188, 2009. https://doi.org/10.1016/j.cmet.2009.08.003
[10] A. Nikolakopoulou, D. Tsakogiannis, et al. Baseline ang-2 serum levels as a predictive factor for survival in nsclc and sclc. Life, vol. 12, no. 12, p. 2092, 2022. https://doi.org/10.3390/life12122092
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