Analytical Data
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Gene name
LECT2
- Application
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Alternative Names
LECT2；Leukocyte cell-derived chemotaxin-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
O14960
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Expression Region
19-151aa
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AA Sequence
GPWANICAGKSSNEIRTCDRHGCGQYSAQRSQRPHQGVDILCSAGSTVYA PFTGMIVGQEKPYQNKNAINNGVRISGRGFCVKMFYIKPIKYKGPIKKGE KLGTLLPLQKVYPGIQSHVHIENCDSSDPTAYL
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Molecular Weight
16 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
LECT2, or leukocyte-derived chemotactic factor 2, is a secreted protein that plays a pivotal role in immune responses and inflammatory processes. Initially identified as a protein expressed by leukocytes, LECT2 has garnered attention due to its involvement in various physiological and pathological contexts, including autoimmune diseases, cancer, and metabolic disorders. Research has shown that LECT2 can modulate the migration and activation of immune cells, suggesting its potential as a therapeutic target. Additionally, studies indicate that altered levels of LECT2 are associated with conditions such as obesity and kidney diseases, prompting investigations into its role in metabolic regulation. The ability of LECT2 to interact with different cell types and impact signaling pathways makes it a compelling subject for further exploration. Recent advancements in recombinant protein technology have facilitated the production and characterization of LECT2, allowing researchers to delve into its functional properties and mechanisms of action. Understanding LECT2's structure-function relationship and its interactions within the immune system could lead to novel insights in immunology and potential therapeutic applications for diseases where immune dysregulation is a key factor.
