Analytical Data
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Gene name
MYLPF
- Application
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Alternative Names
Fast skeletal myosin light chain 2MLC2B
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96A32
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Expression Region
2-169aa
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Molecular Weight
34.9 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
MYLPF (Myosin Light Chain Phosphatase) is a crucial enzyme involved in the regulation of actin-myosin interactions, playing a significant role in muscle contraction and cellular movement. Understanding the structure and function of MYLPF is vital, as dysregulation of this phosphatase is implicated in various cardiovascular diseases and muscle disorders. Recent studies have highlighted the importance of MYLPF in modulating cellular signaling pathways, particularly in the context of inflammation and cell migration. Research into MYLPF has gained momentum due to its potential therapeutic applications; for instance, targeting MYLPF activity could lead to new strategies for treating conditions such as hypertension and heart failure. Furthermore, the development of MYLPF recombinant proteins has opened avenues for in vitro studies and drug discovery, allowing researchers to dissect its regulatory mechanisms and discover small molecules that can modulate its activity. Investigating the expression patterns, post-translational modifications, and interaction networks of MYLPF is essential for developing a comprehensive understanding of its role in cellular physiology and pathophysiology. As the field progresses, elucidating the functional diversity of MYLPF across different cell types and conditions may provide novel insights into muscle biology and disease mechanisms, paving the way for innovative therapeutic approaches.
