Analytical Data
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Gene name
LILRB2
- Application
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Alternative Names
LILRB2；HLA-6.0；HLA class I histocompatibility antigen. alpha chain G
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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
Q8N423
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Expression Region
22-458aa
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AA Sequence
QTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWIT RIRPELVKNGQFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAY PKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEDEHPQCLNSQP HARGSSRAIFSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGV SKKPSLSVQPGPVVAPGESLTLQCVSDVGYDRFVLYKEGERDLRQLPGRQ PQAGLSQANFTLGPVSRSYGGQYRCYGAYNLSSEWSAPSDPLDILITGQI HGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSI HEYPKYQAEFPMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGP SMGSSPPPTGPISTPAGPEDQPLTPTGSDPQSGLGRHVDHHHHHH
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Molecular Weight
49 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
LILRB2, or Leukocyte Immunoglobulin-Like Receptor B2, is a member of the LILR family, which plays a critical role in the regulation of immune responses. Located on the surface of various immune cells, LILRB2 functions as an inhibitory receptor, modulating signals that can either suppress or enhance immune activation. Its interactions with major histocompatibility complex (MHC) molecules and other ligands make it integral to maintaining immune homeostasis, making it a focal point of research in immunology. The study of recombinant LILRB2 proteins has gained momentum, particularly in understanding their role in immune evasion by tumors and pathogens. By elucidating the mechanisms through which LILRB2 regulates immune checkpoints, researchers aim to identify potential therapeutic targets for enhancing anti-tumor immunity and combating infectious diseases. Moreover, recombinant LILRB2 can serve as a valuable tool for developing novel immunotherapeutic strategies, aiming to block its inhibitory signals to drive a more robust immune response. Through structural and functional characterization, scientists are exploring how modulation of LILRB2 activity can lead to improved outcomes in cancer treatments and autoimmune diseases. Thus, the investigation of LILRB2 recombinant protein is not only pivotal for advancing basic immunological knowledge but also holds promise for real-world applications in clinical immunotherapy.
