Analytical Data
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Gene name
bar
- Application
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Alternative Names
bar；BRCA1-associated RING domain Protein 1
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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
Q8TDU6
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Expression Region
1-330aa
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AA Sequence
MTPNSTGEVPSPIPKGALGLSLALASLIITANLLLALGIAWDRRLRSPPAGCFFLSLLLAGLLTGLALPTLPGLWNQSRRGYWSCLLVYLAPNFSFLSLLANLLLVHGERYMAVLRPLQPPGSIRLALLLTWAGPLLFASLPALGWNHWTPGANCSSQAIFPAPYLYLEVYGLLLPAVGAAAFLSVRVLATAHRQLQDICRLERAVCRDEPSALARALTWRQARAQAGAMLLFGLCWGPYVATLLLSVLAYEQRPPLGPGTLLSLLSLGSASAAAVPVAMGLGDQRYTAPWRAAAQRCLQGLWGRASRDSPGPSIAYHPSSQSSVDLDLN
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Molecular Weight
36.8 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
The study of BAR (Bin-Amphiphysin-Rvs) domain-containing proteins has emerged as a significant area of research due to their crucial roles in cellular membrane dynamics and the regulation of various physiological processes. BAR proteins are characterized by their ability to sense and induce membrane curvature, which is vital for processes such as endocytosis, exocytosis, and membrane trafficking. Their unique amphipathic structure allows them to bind to lipid membranes, facilitating the formation of vesicles and other membrane-bound structures. Given their involvement in key cellular functions, dysregulation of BAR proteins has been implicated in several diseases, including cancer, neurodegeneration, and cardiovascular disorders. Recent advances in structural biology and biophysical techniques have enabled researchers to elucidate the molecular mechanisms by which BAR proteins interact with lipids and other cellular components. Understanding these interactions will provide insights into their functional roles in health and disease, making BAR proteins an attractive target for therapeutic interventions. The ongoing exploration of BAR protein dynamics and their regulatory pathways holds promise for novel strategies in drug development and the treatment of various pathological conditions.
