Analytical Data
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Gene name
LIF
- Application
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Alternative Names
LIF；HILDA；Leukemia inhibitory factor
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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
P15018
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Expression Region
23-202aa
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AA Sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF
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Molecular Weight
20 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
LIF (Leukemia Inhibitory Factor) is a multifunctional cytokine belonging to the IL-6 family, renowned for its roles in regulating diverse biological processes such as cell differentiation, immunity, and embryonic development. Its unique ability to maintain pluripotency in embryonic stem cells (ESCs) has made LIF a subject of intense investigation in developmental biology and regenerative medicine. The therapeutic potential of LIF is underscored by its involvement in cancer biology, where it can exhibit both tumor-promoting and suppressive effects depending on the context. The recombinant production of LIF has become increasingly relevant as it allows for the exploration of its biological functions and therapeutic applications in a controlled manner. Advances in molecular cloning techniques and protein expression systems have facilitated the generation of high yields of biologically active LIF, opening avenues for its use in stem cell research and potential clinical applications, such as regenerative therapies and cancer treatment. Recent studies have focused on understanding the signaling pathways activated by LIF and its interaction with other cytokines, providing insights into its complex roles in cellular dynamics. As research progresses, recombinant LIF has emerged as a pivotal tool in elucidating the mechanisms governing stem cell behavior and developing novel therapeutic strategies aimed at tissue repair and regeneration.
