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Recombinant Porcine Tie-2 Fc Chimera Protein, CF

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When Recombinant Porcine Tie-2 Fc Chimera (10488-T2) is immobilized at 0.5 μg/mL (100 μL/well), Recombinant Human Angiopoietin-2 His-tag (623-AN) binds with an ED50 of 0.3-2.7 ng/mL.
2 μg/lane of Recombinant Porcine Tie-2 Fc Chimera Protein (Catalog # 10488-T2) was resolved withSDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized byCoomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity PoSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Porcine Tie-2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Porcine Tie-2 Fc Chimera (Catalog # 10488-T2) is immobilized at 0.5 µg/mL (100 µL/well), Recombinant Human Angiopoietin-2 His-tag  (Catalog # 623-AN) binds with an ED50 of 0.3-2.7 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived porcine Tie-2 protein
Porcine Tie-2
(Ala23-Lys746)
Accession # XP_020918337.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala23
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
107 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
115-133 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.
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 Porcine Tie-2 Fc Chimera Protein, CF

  • angiopoietin-1 receptor
  • CD202b antigen
  • CD202b
  • EC 2.7.10
  • EC 2.7.10.1
  • hTIE2
  • p140 TEK
  • soluble TIE2 variant 1
  • soluble TIE2 variant 2
  • TEK tyrosine kinase, endothelial
  • TEK
  • Tie2
  • Tie-2
  • TIE2CD202b
  • Tunica interna endothelial cell kinase
  • Tyrosine-protein kinase receptor TEK
  • Tyrosine-protein kinase receptor TIE-2
  • venous malformations, multiple cutaneous and mucosal
  • VMCM
  • VMCM1

Background

Tie-1/Tie (tyrosine kinase with Ig and EGF homology domains 1) and Tie-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains, followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region (1). These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis (2). Porcine Tie-2 cDNA encodes a 1124 amino acid (aa) residue precursor protein that shares 94% sequence homology with human Tie-2 in the extracellular domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind Tie-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-2 display similar angiogenesis defects (3).

  1. Partanen, J. and D.J. Dumont (1999) Curr. Top. Microbiol. Immunol. 237:159.
  2. Takakura, N. et al. (1998) Immunity 9:677.
  3. Procopio, W. et al. (1999) J. Biol. Chem. 274:30196.

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