Analytical Data
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Gene name
LRG1
- Application
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Species
Mouse
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q91XL1
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Expression Region
Leu37~Leu342
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Molecular Weight
47kDa
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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
LRG1 (Leucine-rich alpha-2-glycoprotein 1) is a glycoprotein that has gained significant attention in recent years due to its potential role in various biological processes and diseases. Initially identified as a protein associated with acute phase responses, LRG1 has been implicated in inflammatory conditions, cancer, and cardiovascular diseases. Its expression levels have been shown to correlate with disease severity, making it a candidate for diagnostic and prognostic biomarkers. Research indicates that LRG1 may play a role in angiogenesis, tissue repair, and the modulation of immune responses. As a result, the recombinant production of LRG1 has become a focal point for scientists seeking to further understand its functional roles and underlying mechanisms. By expressing LRG1 in suitable systems, researchers can study its biochemical properties, elucidate its interactions with other proteins, and investigate its impact on cellular pathways. Such studies are vital for determining LRG1's therapeutic potential and paving the way for new treatment strategies targeting its associated pathways. Understanding the properties and functions of LRG1 through recombinant technology may ultimately contribute to advancements in precision medicine and the development of novel diagnostic tools.
