Analytical Data
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Gene name
MLKL
- Application
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Alternative Names
MLKL；Mixed lineage kinase domain-like Protein
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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
Q8NB16
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Expression Region
1-471aa
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AA Sequence
MENLKHIITLGQVIHKRCEEMKYCKKQCRRLGHRVLGLIKPLEMLQDQGK RSVPSEKLTTAMNRFKAALEEANGEIEKFSNRSNICRFLTASQDKILFKD VNRKLSDVWKELSLLLQVEQRMPVSPISQGASWAQEDQQDADEDRRAFQM LRRDNEKIEASLRRLEINMKEIKETLRQYLPPKCMQEIPQEQIKEIKKEQ LSGSPWILLRENEVSTLYKGEYHRAPVAIKVFKKLQAGSIAIVRQTFNKE IKTMKKFESPNILRIFGICIDETVTPPQFSIVMEYCELGTLRELLDREKD LTLGKRMVLVLGAARGLYRLHHSEAPELHGKIRSSNFLVTQGYQVKLAGF ELRKTQTSMSLGTTREKTDRVKSTAYLSPQELEDVFYQYDVKSEIYSFGI VLWEIATGDIPFQGCNSEKIRKLVAVKRQQEPLGEDCPSELREIIDECRA HDPSVRPSVDEILKKLSTFSK
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Molecular Weight
59 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
MLKL (Mixed Lineage Kinase Domain-Like Protein) is a crucial effector in the pathway of programmed necrosis, particularly in the context of necroptosis, a form of regulated cell death distinct from apoptosis. Initially identified as a key player in the TNF receptor signaling cascade, MLKL is activated through phosphorylation by the kinases RIPK1 and RIPK3, leading to its oligomerization and subsequent translocation to the plasma membrane. This process disrupts cellular integrity and triggers inflammation, marking its role in various pathological conditions, including neurodegenerative diseases, inflammatory disorders, and cancer. Given its significance in necroptosis, researchers have focused on elucidating the molecular mechanisms governing MLKL function and the implications of its activity in disease contexts. Advances in structural biology have facilitated the characterization of MLKL's oligomeric states and provided insights into its interaction with lipid membranes, which are critical for understanding its role in cell death and inflammation. The development of MLKL inhibitors has emerged as a promising therapeutic strategy to modulate necroptosis, potentially offering avenues for treating diseases where this process is dysregulated. Hence, the study of MLKL, particularly through recombinant protein techniques, is pivotal for both basic biological research and the development of innovative treatments targeting necroptosis-related pathologies.
