Analytical Data
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Gene name
VGLL3
- Application
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Alternative Names
VGLL3; Transcription cofactor vestigial-like protein 3; Vgl-3
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A8MV65
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Expression Region
1-320aa
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Molecular Weight
37.2 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
VGLL3 (Vestigial Like Family Member 3) is a member of the Vestigial-like family of proteins, which are implicated in various cellular processes, including gene regulation, development, and differentiation. Recent research has highlighted the potential role of VGLL3 in cancer biology, particularly in tumor progression and metastasis. VGLL3 has been identified as a co-activator of transcription factors such as TEAD, influencing the expression of genes associated with cell growth and proliferation. The study of VGLL3 as a recombinant protein aims to elucidate its functional mechanisms and interactions at the molecular level. By producing VGLL3 in a recombinant form, researchers can investigate its role in cell signaling pathways, interactions with other proteins, and its impact on cellular phenotypes. Furthermore, understanding VGLL3's structure and function may provide insights into its potential as a therapeutic target in cancer treatment, as its dysregulation has been linked to various malignancies. This research not only contributes to our understanding of VGLL3's biological significance but also opens avenues for exploring its application in targeted therapies and personalized medicine strategies. Overall, the investigation of VGLL3 as a recombinant protein serves to advance our knowledge of its role in health and disease, highlighting its importance in the field of cancer research and potential implications for therapeutic interventions.
