Analytical Data
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Gene name
TIE-2
- Application
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Alternative Names
CD202b; CD202-B; TEK; VMCM1; Tyrosine Kinase With Immunoglobulin Like And EGF Like Domains 2; Venous Malformations Multiple Cutaneous And Mucosal
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 85% as determined by SDS-PAGE.
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Uniprot
Q02763
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Expression Region
Met1~Ile465
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Protein Length
Partial
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Molecular Weight
55kDa
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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.
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Protein Description
TIE-2, also known as TEK receptor tyrosine kinase, plays a critical role in angiogenesis and endothelial cell regulation. It was originally identified as a receptor for angiopoietins, which are molecules that promote blood vessel formation and stabilization. The TIE-2 signaling pathway is essential for vascular development and maintenance, influencing processes such as endothelial cell survival, proliferation, and migration. Research has shown that TIE-2 is implicated in various physiological and pathological conditions, including tumor angiogenesis, cardiovascular diseases, and inflammatory responses. By understanding the molecular mechanisms underlying TIE-2 activity, scientists aim to develop targeted therapies for conditions characterized by abnormal blood vessel formation. The exploration of TIE-2 recombinant proteins enhances our ability to study these pathways, enabling the design of novel therapeutic strategies to modulate endothelial function and improve outcomes in diseases with vascular involvement. Overall, TIE-2 remains a significant focus in vascular biology and drug development, highlighting its potential as a target for innovative therapeutic interventions.











