Analytical Data
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Gene name
ler
- Application
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Alternative Names
ler；ZSCAN11；Zinc finger Protein 232
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Species
E.coli
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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
O87544
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Expression Region
220-463aa
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AA Sequence
GVGDIGSSDYCEKDIVCRVKPSAEFLSASKSVARMVFTPKTGYTGYCSGTLLNNSNSPKRQLFWSAAHCISTQKVANTLQTYWLYDATGCDNDTLSDKAVTLTGGATLLHSHATRDTLLLELKSAPPSGAYYAGWNSSAIATKGTAIEGIHHPSGDLKKYSLGSVTALSSTIDGKKPLTKVAWTTGVTEGGSSGSGLFTISSTSGYQLRGGLYGGTSYCSAPSDPDYYSQLDGVWSSIKTYFSP
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Molecular Weight
52.7 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
The study of LER (Lateral Epithelium-Reinforcing) recombinant proteins has gained significant attention in the field of molecular biology and biotechnology due to their crucial role in cellular processes and potential therapeutic applications. LER proteins are primarily involved in maintaining the structural integrity of epithelial tissues, playing critical roles in cell adhesion, signaling, and tissue homeostasis. Research has shown that these proteins are not only vital for the development and maintenance of epithelial layers but also play a role in pathological conditions, such as cancer metastasis and wound healing. By characterizing and recombinantly producing LER proteins, scientists aim to uncover their functional mechanisms and regulatory pathways. This, in turn, enables the development of novel therapeutic strategies, such as targeted drug delivery systems and tissue engineering applications. Recombinant DNA technology allows for the expression and purification of these proteins in various host systems, facilitating detailed studies of their properties and interactions. As a result, LER recombinant proteins hold promise not only for advancing basic scientific knowledge but also for practical applications in regenerative medicine, diagnostics, and therapeutics. Overall, the exploration of LER recombinant proteins presents a fascinating avenue for understanding epithelial biology and advancing medical science.
