Analytical Data
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Gene name
LILRA5
- Application
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Alternative Names
LILRA5；ILT11；LILRB7；LIR9；Leukocyte immunoglobulin-like receptor subfamily A member 5
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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
A6NI73-1
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Expression Region
1-268aa
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AA Sequence
MAPWSHPSAQ LQPVGGDAVS PALMVLLCLG LSLGPRTHVQ AGNLSKATLW AEPGSVISRG NSVTIRCQGT LEAQEYRLVK EGSPEPWDTQ NPLEPKNKAR FSIPSMTEHH AGRYRCYYYS PAGWSEPSDP LELVVTGFYN KPTLSALPSP VVTSGENVTL QCGSRLRFDR FILTEEGDHK LSWTLDSQLT PSGQFQALFP VGPVTPSHRW MLRCYGSRRH ILQVWSEPSD LLEIPVSGAA DNLSPSQNKS DSGTASHLQD YAVENLIR
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Molecular Weight
27 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
LILRA5, a member of the Leukocyte Immunoglobulin-like Receptor (LILR) family, has garnered significant interest in immunological research due to its potential role in modulating immune responses. This receptor is primarily expressed on myeloid cells and is known to interact with various ligands, including major histocompatibility complex (MHC) molecules. The study of LILRA5 and its recombinant protein forms is pivotal for understanding its function in innate immunity, particularly in regulating inflammation and immune tolerance. Recent discoveries have implicated LILRA5 in several pathological conditions, including autoimmune diseases and infections, suggesting that it may serve as a therapeutic target or biomarker. Researchers are focusing on the expression and purification of LILRA5 recombinant proteins to elucidate their structural properties and binding affinities, which can provide insights into their biological roles. By studying these proteins, scientists aim to unravel the complexities of immune regulation and explore new avenues for treatment strategies in immune-related disorders. The ongoing research in this field underscores the significance of LILRA5 in both basic and translational immunology, highlighting its potential implications in enhancing our understanding of immune mechanisms and developing novel therapeutic interventions.
