Analytical Data
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Gene name
LARGE
- Application
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Alternative Names
Glycosyltransferase-like protein LARGE1; Acetylglucosaminyltransferase-like 1A
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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
O95461
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Expression Region
Thr25~Ala178
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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
The study of large recombinant proteins has become increasingly relevant in various fields, particularly in biotechnology and therapeutic development. Traditionally, the production of proteins for research and clinical applications has been limited by the challenges associated with expressing and purifying large proteins, which often exceed 100 kDa in size. These proteins can exhibit complex structures and elusive biochemical properties, making them critical for the study of many biological processes, including immune responses, enzyme activities, and structural biology. Recent advancements in genetic engineering, expression systems, and purification techniques have enabled scientists to overcome these obstacles, allowing for the successful production of large recombinant proteins. Additionally, these proteins serve as potential candidates for novel therapeutic agents, such as monoclonal antibodies, vaccines, and enzymes for targeted therapies. The ongoing research aims to optimize the expression and purification processes, enhance the yield and functionality of large recombinant proteins, and explore their application in drug development, diagnostics, and molecular biology. This expanding knowledge base is crucial for unlocking the therapeutic potential of large proteins and addressing various diseases, thus highlighting their significance in modern biomedical research.
