Analytical Data
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Gene name
LAIR1
- Application
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Alternative Names
LAIR1;CD305;Leukocyte-associated immunoglobulin-like receptor 1
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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
Q6GTX8
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Expression Region
22-163aa
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AA Sequence
QEEDLPRPSISAEPGTVIPLGSHVTFVCRGPVGVQTFRLERESRSTYNDT EDVSQASPSESEARFRIDSVSEGNAGPYRCIYYKPPKWSEQSDYLELLVK ETSGGPDSPDTEPGSSAGPTQRPSDNSHNEHAPASQGLKAEHVDHHHHHH
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Molecular Weight
17 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
LAIR1 (Lymphocyte Activation Gene-3, also known as CD305) is an inhibitory receptor predominantly expressed on immune cells, particularly lymphocytes. It plays a crucial role in modulating the immune response by limiting excessive activation and maintaining immune homeostasis. LAIR1's interaction with collagen, a prominent extracellular matrix protein, has garnered significant interest due to its potential implications in both autoimmune diseases and cancer. The study of LAIR1, particularly its recombinant protein form, has opened new avenues for understanding its functional mechanisms in immune regulation. Recent research has focused on characterizing LAIR1's structure and its binding properties, which could illuminate its role in cell signaling pathways and its potential as a therapeutic target. Investigating LAIR1's recombinant protein offers insights into developing novel immunotherapies or enhancing existing ones by strategically targeting immune checkpoints. This research is particularly relevant in the context of improving treatment outcomes for diseases characterized by dysregulated immune responses, as well as in the design of biomaterials that mimic the extracellular environment to modulate immune behavior.
