Analytical Data
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Gene name
LCN12
- Application
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Alternative Names
LCN12；Epididymal-specific lipocalin-12
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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
Q6JVE5
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Expression Region
20-192aa
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AA Sequence
Q TPTPLPLPPP MQSFQGNQFQ GEWFVLGLAG NSFRPEHRAL LNAFTATFEL SDDGRFEVWN AMTRGQHCDT WSYVLIPAAQ PGQFTVDHGV EPGADREETR VVDSDYTQFA LMLSRRHTSR LAVLRISLLG RSWLLPPGTL DQFICLGRAQ GLSDDNIVFP DVTGWSPQAS VC
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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
LCN12 (lipocalin 12) is a member of the lipocalin protein family known for its ability to bind small hydrophobic molecules. It is primarily expressed in human tissues, particularly in the skin and lungs, implicating its potential role in various physiological processes such as immune response, cellular trafficking, and tissue homeostasis. Research on LCN12 has gained momentum due to its association with inflammatory conditions and its emerging role in cancer progression, where it may influence tumor microenvironments and interactions with immune cells. The interest in recombinant LCN12 protein has been fueled by its potential applications in therapeutic interventions and diagnostics. Understanding its structure and function at a molecular level can provide insights into its mechanism of action and pave the way for novel treatments targeting LCN12-related pathways. Consequently, studies often focus on the successful expression and purification of recombinant LCN12, ensuring that the protein maintains its biological activity. This foundational research contributes to unraveling the complex biological functions of LCN12, offering opportunities to explore its potential as a biomarker or a therapeutic target in various diseases.
