Analytical Data
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Gene name
LRBA
- Application
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Alternative Names
LRBA；BGL；CDC4L；LBA；Lipopolysaccharide-responsive and beige-like anchor Protein
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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
P50851
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Expression Region
1267-1500aa
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AA Sequence
PQPHRHVLEISRQHEQPGQGIAPDAVNGQRRDSRSTVFRIPEFNWSQMHQRLLTDLLFSIETDIQMWRSHSTKTVMDFVNSSDNVIFVHNTIHLISQVMDNMVMACGGILPLLSAATSATHELENIEPTQGLSIEASVTFLQRLISLVDVLIFASSLGFTEIEAEKSMSSGGILRQCLRLVCAVAVRNCLECQQHSQLKTRGDKALKPMHSLIPLGKSAAKSPVDIVTGGISPV
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Molecular Weight
29.8 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
LRBA (LPS-responsive beige-like anchor protein) is a key player in the immune system, particularly in regulating B cell function and maintaining immune homeostasis. Mutations in the LRBA gene have been linked to a rare immunodeficiency disorder known as LRBA deficiency, characterized by recurrent infections, autoimmunity, and gastrointestinal complications. The study of LRBA and its interactions with other signaling molecules has gained traction, as understanding its function could illuminate the underlying mechanisms of both innate and adaptive immunity. Researchers have focused on LRBA's role in lysosomal trafficking and its influence on antigen presentation, which are critical for effective immune responses. Furthermore, there is growing interest in the potential therapeutic applications of LRBA modulation, including targeted therapies for autoimmune diseases and strategies to enhance vaccine efficacy. Recent advances in structural biology and protein engineering have enabled the characterization of LRBA's structural and functional domains, paving the way for innovative research approaches. Overall, LRBA serves as a vital link between genetic insights and practical applications in immunology, making it a compelling subject for ongoing study and therapeutic exploration.
