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Recombinant Mouse Tie-1 (1-749) Fc Chimera Protein, CF

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When Recombinant Mouse Integrin alpha V beta 3 (7889-AV) is immobilized at 2 µg/mL (100 µL/well), Recombinant Mouse Tie‑1 (1-749) Fc Chimera (Catalog # 11220-TI) binds with an ED50 of 2.00-20.0 μg/mL.
2 μg/lane of Recombinant Mouse Tie-1 (1-749) Fc Chimera Protein (Catalog # 11220-TI) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Tie-1 (1-749) Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Integrin alpha V beta 3  (Catalog # 7889-AV) is immobilized at 2 µg/mL (100 µL/well), Recombinant Mouse Tie-1 (1-749) Fc Chimera (Catalog # 11220-TI) binds with an ED50 of 2.00-20.0 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Tie-1 protein
Mouse Tie-1
(Ser22-Ala749)
Accession # Q06806.3
IEGRMDPMouse IgG2A
(Glu98-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Ser22
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
106 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
105-125 kDa, under reducing conditions.

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Tie-1 (1-749) Fc Chimera Protein, CF

  • EC 2.7.10
  • EC 2.7.10.1
  • JTK14soluble TIE1 variant 3
  • receptor tyrosine kinase
  • soluble TIE1 variant 1
  • soluble TIE1 variant 2
  • soluble TIE1 variant 5
  • Tie1
  • Tie-1
  • TIEsoluble TIE1 variant 4
  • tyrosine kinase with immunoglobulin and epidermal growth factor homologydomains 1
  • tyrosine kinase with immunoglobulin-like and EGF-like domains 1
  • tyrosine-protein kinase receptor Tie-1

Background

Tyrosine -protein kinase with immunoglobulin (Ig) like and epidermal growth factor (EGF) like domains 1 (Tie1), along with the closely related Tie2, is a transmembrane, vascular-specific receptor tyrosine kinase (RTKs) involved in angiogenesis, vascular development, and hematopoiesis (1,2). The Tie molecules are characterized by three Ig-like domains, three EGF-like domains, and three fibronectin type III-like repeats in the extracellular domain (ECD) and a split tyrosine kinase domain in the cytoplasmic region (3,4). The ECD of mouse Tie1 shares 89% amino acid sequence identity with human Tie1. Tie1 is expressed in endothelial and some hematopoietic progenitor cells and helps modulate angiopoietin signaling (5). While Tie1 is unable to directly bind any of the angiopoietins, it can modulate Tie2/angiopoietin signaling through Tie1/Tie2 heterodimer formation (6). Upregulation of Tie1 has been found in some leukemia and tumor related endothelial cells and inhibition of Tie1 has been shown to prevent metastasis and is being studied as a target for anti-angiogenesis treatments (7-9).
  1. Thomas, M. and Augustin, H. (2009) Angiogenesis 12:125.
  2. Fagiani, E. and Christofori, G. (2013) Cancer Letters 328:1.
  3. Seegar, T.C.M. et al. (2010). Mol. Cell. 37:643.
  4. Barton, W.A. et al. (2006). Nat Struc & Molec Biol. 13:524.
  5. Saharinen, P. et al. (2017) Nat Rev Drug Discov. 16:635.
  6. Yuan, H.T. et al. (2007) FASEB J. 21:3171.
  7. Yang, P. et al. (2015). J. Huazhong Univ. Sci. Technol. Med. Sci. 35:615-622.
  8. D'Amico, G. et al. (2014) J Clin Invest. 124:824.
  9. Khan, K.A. and Kerbel, R.S. (2020) EMBO molecular medicine 12:e12355.

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