Analytical Data
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Gene name
PALM
- Application
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Alternative Names
Paralemmin
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75781
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Expression Region
1-384aa
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Molecular Weight
45.7 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
Related Products
Protein Description
PALM (Photo-Activated Localization Microscopy) is a powerful super-resolution imaging technique that allows researchers to visualize proteins and cellular structures at the nanometer scale. The study of recombinant proteins using PALM is crucial for understanding various biological processes at a molecular level. Recombinant proteins are artificially produced through the expression of cloned genes in host cells, allowing for the study of specific protein functions, interactions, and dynamics in real-time. By tagging these proteins with photoactivatable fluorescent markers, PALM can achieve a spatial resolution beyond the diffraction limit of traditional microscopy, enabling the detailed observation of protein localization and interactions within live cells. This technique is particularly valuable in cancer research, neurobiology, and developmental biology, where understanding the spatial and temporal organization of proteins is essential for deciphering complex cellular mechanisms. Recent advancements in PALM have increased its application to study various protein behaviors under physiological conditions, providing insights into protein clustering, signaling pathways, and disease mechanisms. Furthermore, combining PALM with other imaging modalities and biophysical techniques has opened new avenues for investigating dynamic biological processes, making it an indispensable tool in the field of modern molecular biology. As research continues to evolve, the integration of PALM with advances in synthetic biology and bioengineering promises to enhance our understanding of protein function and interaction landscapes, ultimately leading to novel therapeutic strategies for various diseases.
