Analytical Data
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Gene name
MYL2
- Application
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Alternative Names
MYOC;GLC1A;TIGR;Myocilin
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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
P10916
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Expression Region
1-166aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAPKKAKKRA GGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR EMLTTQAERF SKEEVDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD
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Molecular Weight
21 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
MYL2, or Myosin Light Chain 2, is a critical component of the cardiac muscle contraction apparatus and plays a vital role in cardiac physiology. Research into MYL2 has gained significant attention due to its association with various cardiac diseases, particularly hypertrophic cardiomyopathy (HCM), which can lead to heart failure and sudden cardiac death. Mutations in the MYL2 gene have been identified in patients with familial forms of HCM, underscoring its importance in myocardial function and structural integrity. The study and characterization of MYL2 recombinant proteins facilitate a deeper understanding of its biochemical properties, functional dynamics, and interaction with other sarcomere proteins, ultimately providing insights into the molecular mechanisms underlying cardiac muscle contraction. Moreover, recombinant MYL2 proteins serve as valuable tools in the development of therapeutic strategies and interventions aimed at ameliorating the impact of MYL2 mutations in cardiac diseases. This research not only enhances our fundamental understanding of cardiac biology but also holds potential for innovative approaches to treat or prevent heart diseases influenced by MYL2 dysfunction. As such, the continued exploration of MYL2 and its recombinant forms is essential for advancing knowledge in cardiovascular health and disease management.
