Recombinant Human Angiopoietin-2, Biotinylated Protein

Newer Version Available: BT623B
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Discontinued Product

BT623 has been discontinued and is replaced by BT623B.

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Recombinant Human Angiopoietin-2, Biotinylated Protein Summary

Product Specifications

Activity
Measured by its binding ability in a functional ELISA. Immobilized rhTie-2/Fc Chimera at 4 µg/mL (100 µL/well) can bind biotinylated rhAngiopoietin-2 with a linear range of 0.5-100 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Angiopoietin-2 protein
Tyr19-Phe496, with a C-terminal His tag
Accession #
N-terminal Sequence
Analysis
Tyr19
Structure / Form
Oligomer
SDS-PAGE
66 kDa, reducing conditions

Product Datasheets

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BT623

BT623

Formulation Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and CHAPS with BSA as a carrier protein.
Reconstitution

Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Angiopoietin-2

Angiopoietin-2 (Ang-2; also ANGPT2) is a secreted glycoprotein that plays a complex role in angiogenesis and inflammation (1, 2). Mature Ang-2 is 478 amino acids (aa) in length. It contains one coiled-coil domain (aa 166 - 248) that mediates multimerization, and a C-terminal fibrinogen-like domain (aa 275 - 495) that mediates receptor binding. Under reducing conditions, secreted monomeric Ang-2 is 65 - 66 kDa in size. Under nonreducing conditions, both natural and recombinant Ang-2 form 140 kDa dimers, 200 kDa trimers, and 250 - 300 kDa tetramers and pentamers (3 - 6). Alternate splicing generates a short isoform that lacks 52 amino acids (aa) preceding the coiled-coil domain (4). Mature human Ang-2 shares 86% aa sequence identity with mouse and rat Ang-2. Ang-2 is widely expressed during development, but it is restricted postnatally to highly angiogenic tissues such as the placenta, ovaries, and uterus (3). It is particularly abundant in vascular endothelial cells (EC) where it is stored in intracellular Weibel-Palade bodies (1, 3, 7). Both Ang-2 and the related Angiopoietin-1 (Ang-1) are ligands for the receptor tyrosine kinase Tie-2 (2). While Ang-1 is a potent Tie-2 agonist, Ang-2 may act as either a Tie-2 antagonist or agonist, depending upon its state of multimerization. The higher the order of oligomer, the more effective Ang-2 becomes as a Tie-2 agonist (3, 8 - 11). The short isoform appears to block the binding of either Ang-1 or full-length Ang-2 to Tie-2 (4). Ang-2 functions as a pro-angiogenic factor, although it can also induce EC death and vessel regression (12, 13). Upon its release from quiescent EC, it regulates vascular remodeling by promoting EC survival, proliferation, and migration and destabilizing the interaction between EC and perivascular cells (8, 13, 14). Ang-2 is required for postnatal vascular remodeling, and it cooperates with Ang-1 during lymphatic vessel development (7, 15). It mediates the upregulation of ICAM-1 and VCAM-1 on EC, which facilitates the adhesion of leukocytes during inflammation (16). Ang-2 is upregulated in both the endothelium and tumor cells of several cancers as well as in ischemic tissue (17 - 20). Its direct interaction with Integrins promotes tumor cell invasion (21, 22). Ang-2 also promotes the neuronal differentiation and migration of subventricular zone progenitor cells (20).

References
  1. Augustin, H.G. et al. (2009) Nat. Rev. Mol. Cell Biol. 10:165.
  2. Murdoch, C. et al. (2007) J. Immunol. 178:7405.
  3. Maisonpierre, P.C. et al. (1997) Science 27:55.
  4. Kim, I. et al. (2000) J. Biol. Chem. 275:18550.
  5. Procopio, W.N. et al. (1999) J. Biol. Chem. 274:30196.
  6. Kim, K-T. et al. (2005) J. Biol. Chem. 280:20126.
  7. Gale, N.W. et al. (2002) Dev. Cell 3:411.
  8. Yuan, H.T. et al. (2009) Mol. Cell. Biol. 29:2011.
  9. Falcon, B.L. et al. (2009) Am. J. Pathol. 175:2159.
  10. Kim, H-Z. et al. (2009) Biochim. Biophys. Acta 1793:772.
  11. Kim, I. et al. (2001) Cardiovasc. Res. 49:872.
  12. Lobov, I.B. et al. (2002) Proc. Natl. Acad. Sci. 99:11205.
  13. Cao, Y. et al. (2007) Cancer Res. 67:3835.
  14. Nasarre, P. et al. (2009) Cancer Res. 69:1324.
  15. Dellinger, M. et al. (2008) Dev. Biol. 319:309.
  16. Fiedler, U. et al. (2006) Nat. Med. 12:235.
  17. Koga, K. et al. (2001) Cancer Res. 61:6248.
  18. Etoh, T. et al. (2001) Cancer Res. 61:2145.
  19. Tressel, S.L. et al. (2008) Arterioscler. Thromb. Vasc. Biol. 28:1989.
  20. Liu, X.S. et al. (2009) J. Biol. Chem. 284:22680.
  21. Hu, B. et al. (2006) Cancer Res. 66:775.
  22. Imanishi, Y. et al. (2007) Cancer Res. 67:4254.
Entrez Gene IDs
285 (Human); 11601 (Mouse); 89805 (Rat); 396730 (Porcine); 101925495 (Cynomolgus Monkey)
Alternate Names
AGPT2; ANG2; ANG-2; angiopoietin 2; Angiopoietin-2; angiopoietin-2a; angiopoietin-2B; angiopoitin 2; ANGPT2; Tie2-ligand

Citations for Recombinant Human Angiopoietin-2, Biotinylated Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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  1. Directed evolution of an angiopoietin-2 ligand trap by somatic hypermutation and cell surface display.
    Authors: Brindle, Nicholas, Sale, Julian E, Arakawa, Hiroshi, Buerstedde, Jean-Mar, Nuamchit, Teonchit, Sharma, Shikha, Steele, Kathryn
    J Biol Chem, 2013-10-08;288(46):33205-12.
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  2. Engineering a therapeutic IgG molecule to address cysteinylation, aggregation and enhance thermal stability and expression.
    Authors: Buchanan A, Clementel V, Woods R, Harn N, Bowen M, Mo W, Popovic B, Bishop S, Dall'Acqua W, Minter R, Jermutus L, Bedian V
    MAbs, 2013-02-14;5(2):255-62.
    Species: Human
    Sample Types: Protein
    Applications: Functional ELISA

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