Analytical Data
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Gene name
MYL12B
- Application
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Alternative Names
MRLC2; MLC20; SHUJUN-1; Myosin Regulatory Light Chain 2; Myosin regulatory light chain 2-B, smooth muscle isoform; Myosin regulatory light chain 20 kDa
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O14950
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Expression Region
Lys5~Asp172
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Molecular Weight
49kDa
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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
MYL12B, also known as myosin regulatory light chain 12B, is a crucial protein involved in the regulation of smooth muscle contraction and various cellular processes, including cell motility and division. It belongs to the myosin light chain family, which plays a significant role in the contraction mechanism of muscle fibers by modulating the activity of myosin motor proteins. Research on MYL12B has garnered interest in recent years due to its potential implications in various health-related conditions, such as hypertension, cancer metastasis, and other diseases characterized by abnormal cellular movement and contraction. Understanding the structure and function of MYL12B is essential for elucidating its roles in cellular dynamics and disease pathology. The reconstitution of MYL12B as a recombinant protein allows for in-depth studies of its biochemical properties, interactions with other proteins, and its regulatory mechanisms. Advances in recombinant DNA technology have enabled the production of MYL12B in various expression systems, facilitating research into its role in diseases and providing potential therapeutic targets. Furthermore, MYL12B serves as a model to investigate protein phosphorylation and the dynamic regulation of cellular processes, making it a valuable subject for both basic research and translational applications. Overall, the study of MYL12B recombinant protein is critical for enhancing our understanding of muscle physiology and the molecular basis of disease, ultimately contributing to the development of novel therapeutic strategies.
