Analytical Data
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Gene name
LAIR2
- Application
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Alternative Names
LAIR2;CD306;Leukocyte-associated immunoglobulin-like receptor 2
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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
Q6ISS4
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Expression Region
22-152aa
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AA Sequence
QEGALPRPSISAEPGTVISPGSHVTFMCRGPVGVQTFRLEREDRAKYKDS YNVFRLGPSESEARFHIDSVSEGNAGLYRCLYYKPPGWSEHSDFLELLVK ESSGGPDSPDTEPGSSAGTVPGTEASGFDAP
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Molecular Weight
15 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
LAIR2 (Lymphocyte Activation Gene 2) is a protein that plays a crucial role in immune regulation, particularly in the context of its interaction with collagen in the extracellular matrix. The study of LAIR2 focuses on its function as an immunoreceptor, which can modulate the immune response by dampening the activation of lymphocytes, particularly during inflammatory processes. Given the significance of immune modulation in various diseases, including autoimmune disorders and cancer, research on LAIR2 has gained momentum as scientists aim to understand its mechanisms in detail. The reconstitution of LAIR2 as a recombinant protein has facilitated the examination of its structural and functional properties, enabling researchers to explore its binding affinities, downstream signaling pathways, and potential therapeutic applications. By utilizing techniques such as x-ray crystallography and biophysical assays, researchers can elucidate the interactions between LAIR2 and its ligands, offering insights into how it can be harnessed for therapeutic purposes. Overall, the study of LAIR2 and its recombinant form is essential for developing targeted immunotherapies and enhancing our understanding of immune system dynamics.
