Analytical Data
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Gene name
LRRC8A
- Application
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Alternative Names
AGM5; FLJ10337; FLJ41617; KIAA1437; Leucine rich repeat containing 8 family member A; Leucine rich repeat containing protein 8A; Leucine-rich repeat-containing protein 8A; LRC8A_HUMAN; LRRC8; Lrrc8a
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IWT6
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Expression Region
711-810aa
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AA Sequence
QNLAITANRIETLPPELFQCRKLRALHLGNNVLQSLPSRVGELTNLTQIELRGNRLECLPVELGECPLLKRSGLVVEEDLFNTLPPEVKERLWRADKEQA
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Molecular Weight
36.74 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
LRRC8A (Leucine-Rich Repeat Containing 8 A) is a crucial protein that functions as a component of the volume-regulated anion channel (VRAC), playing a significant role in maintaining cellular homeostasis and mediating osmoregulation. Its involvement in various physiological processes, including cell volume regulation, apoptosis, and the immune response, has drawn considerable research interest. Mutations and dysfunctions in LRRC8A have been linked to a number of pathological conditions, including neurological disorders and cancer, emphasizing the need for a deeper understanding of its functional mechanisms. Recent studies have focused on the structural and functional characterization of LRRC8A, exploring its oligomeric nature and regulatory pathways that modulate its activity. Additionally, recombinant LRRC8A proteins are being utilized to elucidate the biophysical properties of the channel and to develop pharmacological tools to target this channel in various diseases. Overall, the thorough investigation of LRRC8A as a model for studying ion channel biology is essential for advancing therapeutic strategies that exploit its potential role in health and disease.
