Analytical Data
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Gene name
MYL5
- Application
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Alternative Names
MYL5;Myosin light chain 5
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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
Q02045
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Expression Region
1-132aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMDQNRDGFIDKEDLKDTYASLGKTNV KDDELDAMLKEASGPINFTMFLNLFGEKLSGTDAEETILNAFKMLDPDGK GKINKEYIKRLLMSQADKMTAEEVDQMFQFASIDVAGNLDYKALSYVITH GEEKEE
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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
MYL5, or Myosin Light Chain 5, is a crucial component of the myosin protein family, which plays a significant role in muscle contraction and various cellular processes involving motility and stability. Research into MYL5 has gained momentum due to its association with cardiomyocyte function and development, as well as potential implications in cardiac diseases. The protein is known to interact with thick filament structures in muscle cells, facilitating the contraction cycle. Recent studies have highlighted its involvement in the regulation of intracellular calcium levels and signaling pathways that influence muscle cell differentiation. Additionally, MYL5 has been implicated in other physiological processes, such as cellular migration and proliferation. Given its fundamental roles, understanding the structure and function of MYL5, particularly through recombinant protein studies, can provide insights into its molecular mechanisms and therapeutic potential. Recombinant MYL5 proteins are valuable for in vitro studies that aim to elucidate the protein’s functional dynamics and interactions with other cellular components, contributing to the broader understanding of myopathies and cardiovascular disorders. As the field continues to explore the complexities of MYL5, it opens avenues for potential interventions in muscle-related diseases and regenerative medicine, marking it as a significant target for future research efforts.
