Analytical Data
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Gene name
vHL
- Application
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Alternative Names
vHL；von Hippel-Lindau disease tumor suppressor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
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Molecular Weight
71.9 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
Von Hippel-Lindau (vHL) syndrome is a hereditary condition characterized by the development of various tumors and cysts in multiple organs, primarily resulting from mutations in the VHL gene. The vHL protein plays a crucial role in the degradation of hypoxia-inducible factor (HIF), a transcription factor that regulates oxygen homeostasis and cellular responses to low oxygen levels. Understanding vHL protein dynamics and its molecular pathways has significant implications for cancer research, particularly in the contexts of clear cell renal cell carcinoma, which is frequently associated with vHL mutations. The study of vHL recombinant proteins enables researchers to elucidate the functional mechanisms of vHL in regulating gene expression and the proteasomal degradation of HIF under normoxic and hypoxic conditions. By producing and analyzing these proteins in vitro, scientists can investigate the structural and functional consequences of specific mutations, providing insights into the pathophysiology of vHL syndrome and its associated tumors. Furthermore, vHL recombinant proteins serve as a valuable tool for developing targeted therapies that can potentially counteract the effects of dysfunctional vHL, offering new avenues for treatment in patients with vHL syndrome and related malignancies.
