Analytical Data
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Gene name
MLKL
- Application
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Alternative Names
(hMLKL)
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NB16
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Expression Region
1-471aa
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Molecular Weight
69.1 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
MLKL (Mixed Lineage Kinase Domain-Like Protein) is a crucial protein involved in the process of necroptosis, a form of programmed cell death. This pathway is distinct from apoptosis and is activated under certain stress conditions, particularly when the tumor necrosis factor (TNF) signaling is disrupted. The study of MLKL has garnered significant interest due to its role in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Researchers have identified that upon activation by receptor-interacting protein kinases (RIPK1 and RIPK3), MLKL undergoes conformational changes, leading to its oligomerization and subsequent translocation to cellular membranes, where it disrupts membrane integrity and induces cell death. Understanding the structure and function of MLKL is essential for elucidating the molecular mechanisms of necroptosis and could reveal new therapeutic targets for treating diseases characterized by dysregulated cell death. Recent advances in recombinant protein technology have allowed for the expression and purification of MLKL, facilitating detailed biophysical and biochemical studies. These studies aim to characterize the oligomeric state of MLKL, its interactions with membrane lipids, and the downstream effects of its activity. Such insights could pave the way for novel strategies in modulating necroptosis, offering potential avenues for intervention in various pathologies where this cell death pathway plays a critical role.
