Analytical Data
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Gene name
MYL3
- Application
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Alternative Names
MYL3；Myosin light chain 3
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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
P08590
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Expression Region
1-195aa
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AA Sequence
MAPKKPEPKKDDAKAAPKAAPAPAPPPEPERPKEVEFDASKIKIEFTPEQIEEFKEAFMLFDRTPKCEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPRQEELNTKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMSS
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Molecular Weight
48.8kDa
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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
MYL3, or myosin light chain 3, is a crucial component of the cardiac muscle contractile apparatus, playing an essential role in regulating cardiac contractility and muscle function. Mutations in the MYL3 gene have been implicated in various cardiomyopathies, particularly familial hypertrophic cardiomyopathy (FHC), which can lead to heart failure and sudden cardiac death. The importance of MYL3 in heart function has driven research to explore the biochemical and biophysical properties of MYL3, including its interactions with other contractile proteins and its role in muscle contraction. Recombinant MYL3 protein studies facilitate the understanding of the molecular mechanisms underlying MYL3-related pathologies and allow for the investigation of potential therapeutic approaches. By expressing and purifying MYL3, scientists can analyze its functional dynamics, characterize its interactions at the molecular level, and assess how mutations affect its normal physiology. This research not only furthers the understanding of cardiomyopathies but also generates insights into muscle biology that may inform the development of novel strategies for diagnosing and treating heart diseases associated with MYL3 mutations.
