Analytical Data
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Gene name
NEBL
- Application
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Alternative Names
LNEBL; Actin-binding Z-disk protein
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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
O76041
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Expression Region
Met1~Ala264
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Molecular Weight
56kDa
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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
NEBL (Nedbrin) is a protein that plays a crucial role in various physiological processes, particularly in the regulation of cardiac function and muscle development. Studies have shown that NEBL interacts with other proteins within the cardiac muscle, contributing to the structural integrity of cardiomyocytes and influencing myocardial contractility. The research surrounding NEBL has gained momentum due to its association with various cardiac pathologies, including cardiomyopathy and heart failure. Understanding the molecular mechanisms and structural characteristics of NEBL is essential for elucidating its role in heart diseases and potentially identifying therapeutic targets. Recent advancements in recombinant protein technology have facilitated the production of NEBL in a controlled environment, allowing for in-depth biochemical and biophysical analyses. By employing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, researchers aim to uncover the three-dimensional structure of NEBL and its functional domains. This information is invaluable for understanding how NEBL functions at the molecular level and its interactions with other cardiac proteins. Overall, the study of NEBL and its recombinant forms holds significant promise for advancing our knowledge of cardiac biology and developing novel interventions for heart diseases.
