Analytical Data
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Gene name
TIE-2
- Application
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Alternative Names
Angiopoietin-1 receptor; CD202b; hTIE2; p140 TEK; Tie2; VMCM
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Species
Human
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q02763-1
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Expression Region
A23-L748
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Molecular Weight
125-140 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
TIE-2, also known as angiopoietin receptor tyrosine kinase, plays a vital role in the regulation of vascular development and angiogenesis. It is primarily expressed in endothelial cells and is crucial for maintaining vascular homeostasis. Studies have shown that TIE-2 is involved in the signaling pathways that modulate blood vessel formation, stability, and integrity, making it a key player in both physiological and pathological conditions, including cancer, ischemia, and inflammatory diseases. The receptor binds to its ligands, angiopoietin-1 and angiopoietin-2, which regulate its activity and influence various biological processes. Research on TIE-2 has garnered interest due to its potential as a therapeutic target. Modulating TIE-2 activity may offer new strategies for treating diseases characterized by abnormal blood vessel formation. Furthermore, understanding the structural and functional properties of TIE-2, including its interactions with ligands and downstream signaling molecules, can provide insights into the mechanisms underlying vascular disorders. Consequently, TIE-2 recombinant protein studies are crucial for developing novel therapeutics aimed at regulating angiogenesis and improving outcomes in conditions like cancer, where tumor survival and growth depend on robust blood vessel formation. The continued exploration of TIE-2 and its pathways will enhance our understanding of vascular biology and may lead to innovative approaches for targeting angiogenesis in various diseases.
