Analytical Data
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Gene name
LYNa
- Application
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Alternative Names
ccdA; H; letA; ECOK12F042; Antitoxin CcdA; LynA; Protein H; Protein LetA
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62552
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Expression Region
1-72aa
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AA Sequence
MKQRITVTVD SDSYQLLKAY DVNISGLVST TMQNEARRLR AERWKAENQE GMAEVARFIE MNGSFADENR DW
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Molecular Weight
8.3 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
LYNa, a novel recombinant protein, has garnered significant attention in the fields of biochemistry and molecular biology due to its therapeutic potential and unique structural properties. Emerging from the need for effective biomedical applications, LYNa has been identified as a promising candidate for various therapeutic interventions, including anti-inflammatory and anti-cancer treatments. The research surrounding LYNa focuses on understanding its molecular mechanisms, stability, and interaction with biological targets. Additionally, advancements in recombinant DNA technology have facilitated the efficient production of LYNa in microbial and eukaryotic systems, allowing for cost-effective and scalable synthesis. The protein's modifiable characteristics enable researchers to tailor its properties for improved efficacy and reduced side effects. Investigations into LYNa's pharmacokinetics and pharmacodynamics are crucial for elucidating its safety and therapeutic profile. Furthermore, preclinical studies are ongoing to explore its potential in clinical settings, with the aim of expanding treatment options for diseases that currently lack effective therapies. As such, LYNa represents a frontier in protein research that bridges the gap between molecular understanding and practical applications in medicine.
