Analytical Data
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Gene name
PARVA
- Application
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Alternative Names
PARVA;MXRA2;Alpha-parvin
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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
Q9NVD7
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Expression Region
1-372aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMATSPQKSPSVPKSPTPKSPPSRKKDD SFLGKLGGTLARRKKAKEVSELQEEGMNAINLPLSPIPFELDPEDTMLEE NEVRTMVDPNSRSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQ VLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKW NVDSVHAKSLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQS RQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLN KLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNV SFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE
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Molecular Weight
45 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
PARVA, also known as Paxillin-Associated Regulator of Vascular Assembly, is a crucial protein implicated in cellular processes such as adhesion, migration, and signal transduction, particularly in vascular development and homeostasis. Research on PARVA has garnered attention for its role in cancer metastasis, where altered expression and function can influence tumor progression and the ability of cancer cells to invade surrounding tissues. Investigations into the structural and functional characteristics of PARVA through recombinant protein studies have provided insights into its interactions with other cellular components, such as focal adhesion proteins and signaling pathways. By utilizing techniques such as molecular cloning and expression in various systems, scientists aim to elucidate the mechanisms by which PARVA regulates cellular behavior and contributes to pathological conditions. The findings have potential implications for developing therapeutic strategies targeting PARVA interactions, thereby enhancing our understanding of not only cancer biology but also broader aspects of cell biology and tissue engineering.
