Analytical Data
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Gene name
MYLK4
- Application
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Alternative Names
MYLK4；SGK085；Myosin light chain kinase family member 4
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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
Q86YV6
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Expression Region
1-388aa
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AA Sequence
MLKVKRLEEFNTCYNSNQLEKMAFFQCREEVEKVKCFLEKNSGDQDSRSR HNEAKEVWSNADLTERMPVKSKRTSALAVDIPAPPAPFDHRIVTAKQGAV NSFYTVSKTEILGGGRFGQVHKCEETATGLKLAAKIIKTRGMKDKEEVKN EISVMNQLDHANLIQLYDAFESKNDIVLVMEYVDGGELFDRIIDESYNLT ELDTILFMKQICEGIRHMHQMYILHLDLKPENILCVNRDAKQIKIIDFGL ARRYKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVIAYMLLSGL SPFLGDNDAETLNNILACRWDLEDEEFQDISEEAKEFISKLLIKEKSWRI SASEALKHPWLSDHKLHSRLNAQKKKNRGSDAQDFVTK
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Molecular Weight
70 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
MYLK4 (Myosin Light Chain Kinase 4) is a member of the myosin light chain kinase family, which plays a critical role in cellular processes such as muscle contraction, cell motility, and signal transduction. As a serine/threonine kinase, MYLK4 specifically phosphorylates the regulatory light chain of myosin, thereby influencing actin-myosin interactions and cellular mechanics. Research into MYLK4 has gained momentum due to its potential implications in various physiological and pathological conditions, including cardiac function, smooth muscle contraction, and certain cancers. It has been observed that alterations in MYLK4 expression and activity can significantly impact cell behavior, making it a target of interest for therapeutic strategies. Understanding the role of MYLK4 at a molecular level can shed light on its contributions to muscle-related diseases and provide insights into therapeutic interventions for cancer and vascular disorders. The production and study of recombinant MYLK4 proteins allow researchers to investigate its biochemical properties, interactions with other molecules, and regulatory mechanisms. Such studies are essential for elucidating the functional role of MYLK4 in health and disease, potentially leading to new avenues for drug development and targeted therapies that exploit the kinase's specific activity.
