Analytical Data
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Gene name
MYL1
- Application
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Alternative Names
MYL1；Myosin light chain 1/3. skeletal muscle isoform
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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
P05976
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Expression Region
3-142aa
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AA Sequence
PKKDVKKP VAAAAAAPAP APAPAPAPAP AKPKEEKIDL SAIKIEFSKE QQDEFKEAFL LFDRTGDSKI TLSQVGDVLR ALGTNPTNAE VRKVLGNPSN EELNAKKIEF EQFLPMMQAI SNNKDQATYE DFVEGLRVFD KE
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Molecular Weight
17 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
MYL1, or Myosin Light Chain 1, is a crucial component of the myosin protein family, playing a key role in muscle contraction and cellular motility. It is predominantly expressed in cardiac and skeletal muscle tissues, where it regulates actin filaments by modulating the activity of myosin II, thus influencing contractile function. Recent studies have highlighted the significance of MYL1 in various pathophysiological conditions, including cardiac hypertrophy, heart failure, and other muscle-related diseases. The ability to produce recombinant MYL1 protein has opened new avenues for functional studies, enabling researchers to investigate its structure-function relationships, interaction with other proteins, and post-translational modifications. Understanding the precise mechanisms by which MYL1 regulates muscle contraction is essential for developing therapeutic strategies for related disorders. Additionally, recombinant MYL1 has potential applications in drug testing and the development of muscle regenerative therapies. Given the complex regulatory roles of MYL1 in cardiac and skeletal muscle physiology, further research into its recombinant production and subsequent functional analysis is vital for advancing our knowledge of muscle biology and enhancing clinical outcomes for patients with muscular and cardiac diseases.
