Analytical Data
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Gene name
LIF
- Application
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Alternative Names
LIF, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P15018
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Expression Region
23-202aa
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Molecular Weight
19.7 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
LIF (Leukemia Inhibitory Factor) is a member of the interleukin-6 (IL-6) cytokine family, playing a crucial role in various biological processes, including cell proliferation, differentiation, and survival. Initially discovered for its ability to prevent the differentiation of murine myeloid leukemia cells, LIF has since garnered attention for its significant influence on pluripotent stem cells, particularly in maintaining the self-renewal capabilities of embryonic stem cells. Additionally, LIF is involved in key processes such as inflammation and neural development, making it relevant for both developmental biology and therapeutic applications. The recombinant form of LIF has been extensively studied for its potential in regenerative medicine, particularly in the context of nerve injury and repair, as well as in enhancing the generation of induced pluripotent stem cells (iPSCs). Research into LIF's mechanisms and interactions at the molecular level continues to unfold, with implications for treating a variety of conditions, including neurodegenerative diseases and cancer. The production and characterization of recombinant LIF proteins have become essential in the quest to harness their therapeutic potential, opening pathways for novel treatments and interventions in regenerative and clinical medicine.
