Analytical Data
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Gene name
LMOD3
- Application
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Alternative Names
LMOD3; Leiomodin-3; Leiomodin; fetal form
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q0VAK6
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Expression Region
1-236aa
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AA Sequence
MSEHSRNSDQEELDEEINEDEILANLSAEELKELQSEMEVMAPDPSLPVGMIQKDQTDKPPTGNFNHKSLVDYMYWEKASRRMLEEERVPVTFVKSEEKTQEEHEEIEKRNKNMAQYLKEKLNNEIVANKRESKGSSNIQETDEEDEEEEDDDDDDEGEDDGEESEETNREEEGKAKEQIRNCENNCQQVTDKAFKEQRDRPEAQEKKKKKISQGKIIFRKNNVRAQQKFRSRRTR
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Molecular Weight
54.2 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
The LMOD3 protein, part of the leiomodin family, plays a crucial role in muscle development, particularly in striated muscles such as skeletal and cardiac muscle. It is known to be a modulator of actin filament nucleation and stabilization, which are essential processes in muscle contraction and structural integrity. Research on LMOD3 has gained momentum due to its potential implications in understanding muscle-related diseases, including myopathies and cardiomyopathies. The exploration of LMOD3 as a recombinant protein has been driven by the need to elucidate its functional mechanisms and interactions within the muscle fibers. Recombinant LMOD3 enables detailed biochemical and biophysical studies, allowing researchers to investigate its role in actin dynamics, filament organization, and overall muscle physiology. Furthermore, studying LMOD3 provides insights into its evolutionary conservation and functional diversity across different species, which may contribute to developing novel therapeutic strategies for muscular disorders. Understanding LMOD3's structure-function relationship through advanced techniques such as X-ray crystallography and cryo-electron microscopy could lead to breakthroughs in muscle research, ultimately enhancing our comprehension of muscle biology and pathology.
