Analytical Data
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Gene name
CACNa1H
- Application
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Alternative Names
CACNA1HB; Cav3.2; Low-voltage-activated calcium channel alpha1 3.2 subunit; Voltage-gated calcium channel subunit alpha Cav3.2
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O88427
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Expression Region
Ser2160~Val2359
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Molecular Weight
51kDa
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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
CACNA1H, a gene encoding the alpha-1H subunit of the T-type calcium channel CaV3.2, plays a crucial role in various physiological processes, including neurotransmitter release, muscle contraction, and the regulation of cardiac rhythms. Abnormalities and mutations in CACNA1H have been linked to several neurological and cardiovascular disorders, such as epilepsy, migraine, and cardiac arrhythmias. Given the significance of T-type calcium channels in the generation of rhythmic electrical activity in neurons and cardiac tissues, researchers have focused on characterizing the biophysical properties and pharmacological profiles of the CACNA1H protein. The expression of recombinant CACNA1H in heterologous systems allows for in-depth studies of its functional attributes, helping to elucidate its role in pathophysiological conditions. This research not only furthers our understanding of calcium signaling mechanisms but also has potential implications for developing targeted therapies for related diseases. Understanding the structure-function relationship of CACNA1H can assist in designing selective modulators, which could revolutionize treatment strategies for calcium channel-related disorders.
