Analytical Data
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Gene name
VASP
- Application
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Alternative Names
VASP；Vasodilator-stimulated phosphoProtein
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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
P50552
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Expression Region
1-343aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSD
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Molecular Weight
38 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
Related Products
Protein Description
VASP (Vasodilator-Stimulated Phosphoprotein) is a key regulatory protein involved in various cellular processes, particularly in cytoskeletal dynamics and cell migration. It plays a significant role in the remodeling of actin filaments, which are essential for maintaining cell structure, facilitating motility, and participating in signal transduction pathways. Researchers have focused on recombinant VASP proteins to uncover their functional mechanisms and interactions with other signaling molecules. The production of VASP as a recombinant protein allows for detailed in vitro studies on its phosphorylation status, binding properties, and influence on actin polymerization. Furthermore, understanding VASP's role in pathological conditions such as cancer metastasis and cardiovascular diseases has garnered attention, making it a significant target for therapeutic interventions. The elucidation of VASP's role in cellular mechanics through advanced biochemical and biophysical methods has the potential to provide insights into its contribution to health and disease, highlighting the importance of VASP-recombinant protein studies in biochemistry and molecular biology.
