Analytical Data
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Gene name
MARCKSL1
- Application
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Alternative Names
MARCKS-like protein 1 Macrophage myristoylated alanine-rich C kinase substrate
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49006
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Expression Region
1-195aa
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Molecular Weight
46.5 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
MARCKSL1 (myristoylated alanine-rich C kinase substrate-like protein 1) is an intriguing protein that has garnered attention due to its involvement in various cellular processes, including cell motility, signal transduction, and the regulation of actin cytoskeleton dynamics. As a member of the MARCKS family, MARCKSL1 is characterized by its ability to bind to and modulate the activity of various signaling molecules, particularly those associated with protein kinase C (PKC) pathways. Research has shown that MARCKSL1 plays a critical role in inflammatory responses and cancer progression, acting as a mediator between cellular signaling and changes in cell behavior. Its unique structure, featuring myristoylation and an alanine-rich domain, facilitates its interactions with membranes and other proteins, making it a key player in cellular compartmentalization. Understanding the mechanisms by which MARCKSL1 operates can provide insights into the pathophysiology of diseases where cell migration and signal transduction are disrupted. Consequently, the recombinant expression of MARCKSL1 allows for detailed structural and functional studies, paving the way for potential therapeutic interventions targeting this protein in inflammatory diseases and cancers. The ongoing investigation into MARCKSL1 will not only enhance our understanding of its biological functions but also contribute to the broader field of cell biology and therapeutic development.
