Analytical Data
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Gene name
MYL12A
- Application
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Alternative Names
MYL12A;MLCB;MRLC3;RLC;Myosin regulatory light chain 12A
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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
P19105
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Expression Region
1-171aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMSSKRTKTKTKKRPQRATSNVFAMFD QSQIQEFKEAFNMIDQNR DGFIDKEDLHDMLASLGKNPTDEYLDAMMN EAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQE DYL RELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD
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Molecular Weight
22 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
MYL12A, also known as myosin light chain 12A, is an essential component of the contractile apparatus in various muscle and non-muscle cells. It plays a crucial role in the regulation of smooth muscle contraction and cytokinesis in dividing cells. Research into MYL12A has gained momentum due to its involvement in several physiological and pathological processes, including vascular function, cell motility, and tumor progression. Dysregulation of MYL12A has been linked to various diseases, such as hypertension and cancer, making it a potential therapeutic target. Recent studies employing recombinant MYL12A proteins have facilitated a deeper understanding of its structural and functional properties, as well as its interactions with other cellular proteins. These advances are crucial for elucidating the mechanisms of muscle contraction and cell dynamics. By generating and characterizing recombinant MYL12A, researchers aim to explore its role in cellular processes and its potential implications in disease pathology, paving the way for novel diagnostic and therapeutic strategies.
