Analytical Data
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Gene name
VOPP1
- Application
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Alternative Names
VOPP1；ECOP；WW domain binding Protein VOPP1
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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
Q96AW1
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Expression Region
1-172aa
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AA Sequence
MRRQPAKVAALLLGLLLECTEAKKHCWYFEGLYPTYYICRSYEDCCGSRCCVRALSIQRLWYFWFLLMMGVLFCCGAGFFIRRRMYPPPLIEEPAFNVSYTRQPPNPGPGAQQPGPPYYTDPGGPGMNPVGNSMAMAFQVPPNSPQGSVACPPPPAYCNTPPPPYEQVVKAK
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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
VOPP1, or Vesicular Overexpressed in Pancreatic Cancer 1, is a cytoplasmic protein that has gained attention in recent years due to its potential role in various cellular processes, particularly its involvement in tumor progression and immune response modulation. Initially identified in pancreatic cancer tissues, VOPP1 has been implicated in promoting cell proliferation, survival, and migration, making it a significant factor in cancer biology. Its overexpression has been correlated with poor prognosis in several cancer types, highlighting its potential as a biomarker for malignancy and a target for therapeutic intervention. Moreover, VOPP1 appears to interact with several signaling pathways, including those related to inflammation and apoptosis, which positions it as a crucial player in the tumor microenvironment. Researchers are currently focused on characterizing the structure and function of VOPP1, investigating its exact mechanisms of action, and exploring its role in the regulation of immune cell activities. Understanding VOPP1's function could provide insights into novel cancer treatment strategies and enhance our comprehension of its contributions to tumorigenesis and immune modulation. Thus, the study of VOPP1 and its recombinant protein forms is pivotal in unraveling its potential therapeutic implications and establishing its relevance in cancer biology and medicine.
