Analytical Data
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Gene name
BK
- Application
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Alternative Names
BK；BRADYB1；B1 bradykinin receptor
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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
P46663
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Expression Region
1-353aa
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AA Sequence
MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLLVFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKANLFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQAVPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRCGGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFFAFTNSSLNPVIYVFVGRLFRTKVWELYKQCTPKSLAPISSSHRKEIFQLFWRN
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Molecular Weight
40.4 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
BK (Big Potassium) channel proteins are crucial components in cellular physiology, playing a significant role in regulating various physiological processes, including neuronal excitability, muscle contraction, and vascular smooth muscle function. The research on BK channel proteins has garnered interest due to their involvement in diverse pathophysiological conditions such as hypertension, neurodegenerative diseases, and cardiac dysfunction. These large conductance calcium-activated potassium channels are activated by intracellular calcium levels and membrane depolarization, leading to potassium efflux, which hyperpolarizes the cell and contributes to the regulation of vascular tone and neurotransmitter release. Understanding the structure, function, and regulation of BK channels can provide insights into their role in health and disease, offering potential therapeutic targets for drug development. Recent advancements in molecular biology and structural biology techniques, including cryo-electron microscopy and X-ray crystallography, have enabled researchers to elucidate the intricate mechanisms of BK channel activation and modulation, paving the way for novel interventions aimed at optimizing channel function and addressing related disorders. The ongoing investigation into BK channel interactors and their regulatory pathways is crucial for developing strategies to manipulate these channels effectively, thereby harnessing their therapeutic potential in various clinical settings.
