Cynomolgus Recombinant ANGPT1 protein, hFc Tag (V2LY-0526-LY1371)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Cynomolgus
Tag
hFc Tag
Protein Construction
This product is Cynomolgus Recombinant ANGPT1 protein, hFc Tag consist of Amino Acid: 277-498 and predicts a molecular mass of 54.1 kDa.
Molecule Mass
54.1 kDa
Sequence
Amino Acid: 277-498
Species
Cynomolgus

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>90% as determined by SDS-PAGE.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Angiopoietin 1
Function
Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme.
Biological Process
Activation of transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
Angiogenesis Source: GO_Central
Cell differentiation Source: UniProtKB-KW
Cell-substrate adhesion Source: Ensembl
Glomerulus vasculature development Source: UniProtKB
Hemopoiesis Source: Ensembl
Heparin biosynthetic process Source: UniProtKB
In utero embryonic development Source: Ensembl
Leukocyte migration Source: Reactome
MAPK cascade Source: Reactome
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cell adhesion Source: UniProtKB
Negative regulation of cytokine production involved in immune response Source: Ensembl
Negative regulation of endothelial cell apoptotic process Source: UniProtKB
Negative regulation of neuron apoptotic process Source: Ensembl
Negative regulation of protein import into nucleus Source: Ensembl
Negative regulation of protein phosphorylation Source: Ensembl
Negative regulation of vascular permeability Source: UniProtKB
Positive chemotaxis Source: UniProtKB
Positive regulation of blood-brain barrier permeability Source: ARUK-UCL
Positive regulation of blood vessel endothelial cell migration Source: UniProtKB
Positive regulation of cell adhesion Source: Ensembl
Positive regulation of endothelial cell migration Source: UniProtKB
Positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
Positive regulation of gene expression Source: ARUK-UCL
Positive regulation of peptidyl-serine phosphorylation Source: Ensembl
Positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
Positive regulation of protein kinase B signaling Source: UniProtKB
Positive regulation of protein phosphorylation Source: ARUK-UCL
Positive regulation of protein ubiquitination Source: UniProtKB
Positive regulation of receptor internalization Source: UniProtKB
Protein localization to cell surface Source: UniProtKB
Regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
Regulation of macrophage migration inhibitory factor signaling pathway Source: Ensembl
Regulation of protein binding Source: Ensembl
Regulation of skeletal muscle satellite cell proliferation Source: UniProtKB
Regulation of tumor necrosis factor production Source: Ensembl
Sprouting angiogenesis Source: UniProtKB
Tie signaling pathway Source: UniProtKB
Cellular Location
Secreted
PTM
Glycosylated.

Salimi, U., Menden, H. L., Mabry, S. M., Xia, S., & Sampath, V. (2021). Angiopoietin-1 protects against endotoxin-induced neonatal lung injury and alveolar simplification in mice. Pediatric Research, 1-11.

Chen, X. X., Tang, L., Han, Z. H., Wang, W. J., & Meng, J. G. (2019). Coculture with bone marrow‑derived mesenchymal stem cells attenuates inflammation and apoptosis in lipopolysaccharide‑stimulated alveolar epithelial cells via enhanced secretion of keratinocyte growth factor and angiopoietin‑1 modulating the Toll‑like receptor‑4 signal pathway. Molecular medicine reports, 19(3), 1891-1902.

d'Apolito, M., Santacroce, R., Colia, A. L., Cordisco, G., Maffione, A. B., & Margaglione, M. (2019). Angiopoietin‐1 haploinsufficiency affects the endothelial barrier and causes hereditary angioedema. Clinical & Experimental Allergy, 49(5), 626-635.

Moxon, J. V., Trollope, A. F., Dewdney, B., de Hollander, C., Nastasi, D. R., Maguire, J. M., & Golledge, J. (2019). The effect of angiopoietin-1 upregulation on the outcome of acute ischaemic stroke in rodent models: a meta-analysis. Journal of Cerebral Blood Flow & Metabolism, 39(12), 2343-2354.

Cho, I. A., Lee, Y. J., Lee, H. J., Choi, I. Y., Shin, J. K., Lee, S. A., ... & Choi, W. J. (2018). Angiopoietin-1 and-2 and vascular endothelial growth factor expression in ovarian grafts after cryopreservation using two methods. Clinical and experimental reproductive medicine, 45(3), 143.

Bafunno, V., Firinu, D., D'Apolito, M., Cordisco, G., Loffredo, S., Leccese, A., ... & Margaglione, M. (2018). Mutation of the angiopoietin-1 gene (ANGPT1) associates with a new type of hereditary angioedema. Journal of Allergy and Clinical Immunology, 141(3), 1009-1017.

Loganathan, K., Salem Said, E., Winterrowd, E., Orebrand, M., He, L., Vanlandewijck, M., ... & Jeansson, M. (2018). Angiopoietin-1 deficiency increases renal capillary rarefaction and tubulointerstitial fibrosis in mice. PloS one, 13(1), e0189433.

Kim, K. H., Nakaoka, Y., Augustin, H. G., & Koh, G. Y. (2018). Myocardial angiopoietin-1 controls atrial chamber morphogenesis by spatiotemporal degradation of cardiac jelly. Cell reports, 23(8), 2455-2466.

Thomson, B. R., Souma, T., Tompson, S. W., Onay, T., Kizhatil, K., Siggs, O. M., ... & Quaggin, S. E. (2017). Angiopoietin-1 is required for Schlemm’s canal development in mice and humans. The Journal of clinical investigation, 127(12), 4421-4436.

Michael, I. P., Orebrand, M., Lima, M., Pereira, B., Volpert, O., Quaggin, S. E., & Jeansson, M. (2017). Angiopoietin-1 deficiency increases tumor metastasis in mice. BMC cancer, 17(1), 1-12.

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For research use only. Not intended for any clinical use.

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