Analytical Data
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Gene name
MYLC2PL
- Application
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Alternative Names
MYL10; MYLC2PL; PLRLC; Myosin regulatory light chain 10; Myosin light chain 2; lymphocyte-specific; Precursor lymphocyte-specific regulatory light chain
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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
Q9BUA6
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Expression Region
1-226 aa
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AA Sequence
MLLRLVSNSW PQVILPPRPP KVLGLQAPRR ARKRAEGTAS SNVFSMFDQS QIQEFKESLA LSPRLERNGM ISAHCNLCLT GSSNSPASAS QAFTIMDQNR DGFIDKEDLR DTFAALGRIN VKNEELEAMV KEAPGPINFT VFLTMFGEKL KGTDPEETIL HAFKVFDTEG KGFVKADVIK EKLMTQADRF SEEEVKQMFA AFPPDVCGNL DYRNLCYVIT HGEEKD
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Molecular Weight
25.3 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
MYLC2PL is a recombinant protein derived from the MYLC2 gene, which encodes the regulatory light chain of myosin in cardiac muscle. The significance of MYLC2PL research lies in its potential implications for understanding cardiac muscle function and the molecular mechanisms underlying heart diseases. Abnormalities in myosin light chain phosphorylation can lead to various cardiac dysfunctions, including hypertrophic cardiomyopathy and heart failure. By studying MYLC2PL, researchers aim to elucidate the protein's role in muscle contraction, cellular signaling, and its interactions with other contractile proteins. Additionally, the exploration of MYLC2PL can contribute to the development of therapeutic strategies targeting cardiac conditions, providing insights into gene therapies and protein-engineering approaches. Advances in methods such as CRISPR and recombinant DNA technology have facilitated the production and analysis of MYLC2PL, enabling scientists to investigate its structure-function relationships and post-translational modifications in detail. Overall, the study of MYLC2PL is vital for expanding our understanding of cardiac physiology and pathology, potentially leading to innovative treatments for heart disease.
