Analytical Data
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Gene name
LRRN1/NLRR-1
- Application
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Alternative Names
Neuronal leucine-rich repeat protein 1 ;NLRR-1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6UXK5
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Expression Region
26-631aa
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Molecular Weight
84.3 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
LRRN1/NLRR-1, a member of the leucine-rich repeat protein family, has gained attention in recent years due to its potential roles in various biological processes, particularly in the immune response and developmental regulation. This protein is predominantly expressed in the nervous system and has been implicated in neuroinflammatory diseases and tissue repair mechanisms. Research indicates that LRRN1/NLRR-1 may modulate signaling pathways associated with innate immunity, suggesting its involvement in the body's defense against pathogens. Additionally, studies have shown its potential interactions with other proteins, which could influence cellular functions and responses to environmental stimuli. Given the increasing prevalence of immune-related disorders, characterizing the recombinant forms of LRRN1/NLRR-1 could provide valuable insights into its functional roles and therapeutic potential. The production of recombinant LRRN1/NLRR-1 allows researchers to explore its structural and functional properties, paving the way for future studies aimed at understanding its mechanisms of action in health and disease. Overall, the investigation of LRRN1/NLRR-1 as a recombinant protein could reveal novel pathways for intervention in neuroinflammatory conditions and foster the development of targeted therapies.
