Analytical Data
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Gene name
MRLC2
- Application
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Alternative Names
MRLC2;MYLC2B
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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
O14950
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Expression Region
1-172 aa
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AA Sequence
MSSKKAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDAYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD
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Molecular Weight
26.7 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
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Protein Description
MRLC2, or Myosin Regulatory Light Chain 2, is a critical component of the myosin II motor protein complex, which plays a vital role in various cellular processes, including muscle contraction, cellular motility, and cytokinesis. The regulation of MRLC2 through phosphorylation is essential for its function, as it modulates the interaction between myosin II and actin filaments, thereby influencing contractile dynamics. Research on MRLC2 has gained attention due to its involvement in several physiological processes and its implications in various diseases, such as cancer metastasis and cardiovascular disorders. The dysregulation of MRLC2 phosphorylation can lead to impaired cellular functions, highlighting the importance of understanding its biochemical properties and regulatory mechanisms. Moreover, studying MRLC2 and its signaling pathways can provide valuable insights into potential therapeutic targets for diseases associated with aberrant myosin activity. Consequently, the generation of MRLC2 recombinant proteins has become a significant focus, as these proteins can be utilized in biochemical assays to dissect the molecular mechanisms governing its function and regulation. This research avenue aims to elucidate the intricate roles of MRLC2 in cellular behavior, ultimately contributing to the development of novel therapeutic strategies for related diseases.
