Analytical Data
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Gene name
PVRL2
- Application
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Alternative Names
PVRL2；HVEB；PRR2；PVRL2；Nectin-2
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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
Q92692
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Expression Region
32-360aa
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AA Sequence
QDVRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDAPANHQNVAAFHPKMGPSFPSPKPGSERLSFVSAKQSTGQDTEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVIAKPKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSVRYPPEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQVIFVRETPNTAGAGATGG
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Molecular Weight
39.2kDa
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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
PVRL2, also known as poliovirus receptor-like 2, is a member of the immunoglobulin superfamily and plays a critical role in cell adhesion and signal transduction. It is primarily expressed in various tissues, including the brain and epithelial cells, and has been implicated in several biological processes, such as cell migration and differentiation. Research has identified PVRL2 as a receptor for certain viruses, including the human adenovirus, suggesting its significance in viral pathogenesis. Additionally, abnormal expression of PVRL2 has been associated with various pathological conditions, including certain cancers, where it may contribute to tumor growth and metastasis. Recent studies have focused on understanding the molecular mechanisms underlying PVRL2 function, its interactions with other cellular proteins, and its potential as a therapeutic target. The exploration of PVRL2 as a recombinant protein aims to elucidate its structural characteristics and functional properties, to further investigate its role in disease. Understanding PVRL2’s function at the molecular level may provide insights into its potential applications in diagnostics and therapeutics, particularly in the context of viral infections and malignancies.
