Analytical Data
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Gene name
VASH2
- Application
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Alternative Names
Vasohibin-like protein
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86V25
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Expression Region
1-355aa
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Molecular Weight
56.4 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
Related Products
Protein Description
VASH2 (Vasohibin-2) is a member of the vasohibin family of proteins known for their role in angiogenesis and vascular homeostasis. Research into VASH2 has garnered interest due to its potential implications in various physiological and pathological processes, particularly in tumor biology. VASH2 functions as an angiogenesis inhibitor, influencing endothelial cell behavior and vascular network formation. Elevated levels of VASH2 have been linked to certain cancers, suggesting that it could serve as a biomarker for disease progression or a therapeutic target. Studies involving the recombinant expression of VASH2 protein have focused on elucidating its molecular mechanisms and interactions with other signaling pathways. By characterizing its structure and function, researchers aim to better understand its role in endothelial cell regulation, as well as its potential contributions to tumor growth and metastasis. Furthermore, understanding VASH2's involvement in vascular diseases can lead to new strategies in the treatment of conditions characterized by abnormal blood vessel formation. Overall, the investigation of VASH2 recombinant protein not only enhances our knowledge of its biological functions but also holds promise for developing novel therapeutic approaches in oncology and vascular medicine.
