Analytical Data
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Gene name
VHL
- Application
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Alternative Names
Protein G7 pVHL
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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 90% as determined by SDS-PAGE.
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Uniprot
P40337
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Expression Region
1-213aa
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Molecular Weight
28.2 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
VHL (Von Hippel-Lindau) disease is a hereditary cancer syndrome characterized by the development of various tumors, particularly in the kidneys and central nervous system, due to mutations in the VHL gene. This gene encodes a protein that plays a crucial role in the regulation of hypoxia-inducible factors (HIFs), which are essential for cellular responses to low oxygen levels. Under normoxic conditions, the VHL protein facilitates the ubiquitination and subsequent degradation of HIFs, thereby preventing the activation of genes that promote angiogenesis and cell proliferation. However, mutations in the VHL gene lead to the stabilization of HIFs, resulting in uncontrolled cell growth and increased tumor risk. Research into the recombinant VHL protein has gained momentum as scientists seek to understand its structural and functional properties. This protein holds potential not only as a biomarker for VHL disease but also as a therapeutic target for strategies aimed at modulating HIF activity in various cancers. Studying VHL protein interactions and its role in the ubiquitin-proteasome pathway is vital for uncovering the underlying mechanisms of VHL-associated malignancies and developing novel intervention strategies. Advances in recombinant protein technology enable the production of functional VHL protein, allowing for in-depth biochemical analyses and the exploration of VHL’s interactions with other cellular components. Overall, the investigation of recombinant VHL protein is integral to elucidating the pathophysiology of VHL disease, enhancing our understanding of tumor biology, and paving the way for innovative therapeutic approaches.
