Analytical Data
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Gene name
VCC1
- Application
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Alternative Names
VCC1；VCC1；C-X-C motif chemokine 17
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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
Q6UXB2
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Expression Region
22-119aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL
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Molecular Weight
14 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
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Protein Description
VCC1, a recombinant protein derived from the Vcapsid protein of certain plant viruses, has garnered significant attention in the field of molecular biology and biotechnology due to its potential applications in vaccine development and gene delivery systems. The study of VCC1 is rooted in the understanding of how viral capsids can be engineered to carry payloads, such as antigens or nucleic acids, into host cells effectively. Research has demonstrated that VCC1 retains the structural integrity and immunogenic properties of its viral origins while allowing for modifications that enhance its safety and efficacy for therapeutic use. As a non-replicating entity, VCC1 minimizes the risk associated with traditional virus-based vectors, making it an appealing alternative in developing vaccines against various pathogens. Furthermore, its ability to elicit strong immune responses positions VCC1 as a promising candidate in the design of novel prophylactic and therapeutic strategies. Investigations into the expression, purification, and functional analysis of VCC1 continue to unveil its potential, paving the way for innovative approaches to combat infectious diseases and improve vaccine technologies. This research is not only pivotal in advancing our understanding of viral biology but also holds significant promise for practical applications in medicine and public health.
