Analytical Data
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Gene name
LECT1
- Application
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Alternative Names
CNMD;CHMI;LECT1;MYETS1;Leukocyte cell-derived chemotaxin 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
O75829
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Expression Region
1-334aa
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AA Sequence
MTENSDKVPIALVGPDDVEFCSPPAYATLTVKPSSPARLLKVGAVVLISG AVLLLFGAIGAFYFWKGSDSHIYNVHYTMSINGKLQDGSMEIDAGNNLET FKMGSGAEEAIAVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVGAVTKQ SISSKLEGKIMPVKYEENSLIWVAVDQPVKDNSFLSSKVLELCGDLPIFW LKPTYPKEIQRERREVVRKIVPTTTKRPHSGPRSNPGAGRLNNETRPSVQ EDSQAFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPL GGYYPWPYNYQGCRSACRVIMPCSWWVARILGMV
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Molecular Weight
64 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
LECT1, or Lectin-like domain containing 1, is a protein that has garnered attention in recent years due to its potential roles in various biological processes, including cell signaling and immune responses. Initially identified in studies focused on carbohydrate-binding proteins, LECT1 has been implicated in diverse physiological and pathological conditions, such as inflammation, metabolic disorders, and even cancer. Research suggests that LECT1 may influence cellular interactions and activate signaling pathways that modulate immune cell function, making it a significant molecule in understanding disease mechanisms. Furthermore, its expression patterns and functional significance in different tissues have raised questions about its involvement in tissue regeneration and repair. The ongoing investigation into LECT1 is vital for uncovering its precise biological functions and therapeutic potentials, especially considering its promise as a biomarker for certain diseases. Current studies aim to elucidate the molecular mechanisms by which LECT1 exerts its effects and to explore its potential as a target for novel therapies.
