Analytical Data
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Gene name
PARVA/alpha-Parvin
- Application
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Alternative Names
rHualpha-Parvin, His; PARVA; MXRA2; alpha-Parvin
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Species
Human
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Source
E. coli
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9NVD7-1
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Expression Region
M1-E372
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AA Sequence
MATSPQKSPSVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSELQEEGMNAINLPLSPIPFELDPEDTMLEENEVRTMVDPNSRSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVEHHHHHH
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Protein Length
Full Length of Isoform-1
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Molecular Weight
50 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 alpha-Parvin, is a member of the Parvin family of proteins, which play crucial roles in cellular adhesion and signaling pathways. These proteins are primarily involved in the formation of focal adhesions, where cells adhere to the extracellular matrix, facilitating communication between the inside of the cell and the surrounding environment. Research on PARVA has gained momentum due to its implications in various biological processes, including cell migration, proliferation, and differentiation. Dysregulation of PARVA expression or function has been linked to several pathologies, notably cancer, where altered cell adhesion and migration can contribute to tumor progression and metastasis. Through recombinant protein studies, scientists aim to elucidate the molecular mechanisms by which PARVA interacts with other proteins and facilitates the assembly of signaling complexes at focal adhesions. Understanding these interactions at a structural and functional level can provide insights into the role of PARVA in health and disease. The study of PARVA not only enhances our understanding of fundamental cell biology but also holds potential for the development of therapeutic strategies targeting diseases linked to aberrant PARVA function. Thus, the exploration of PARVA/alpha-Parvin as a recombinant protein offers a promising avenue for advancing our knowledge of its biological significance and therapeutic potential.
