Analytical Data
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Gene name
Leu
- Application
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Alternative Names
Leu；LEU1；T-cell surface glycoProtein CD5
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Species
Human
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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
P06127
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Expression Region
1-495aa
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AA Sequence
MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQCGSVNSYRVLDAGDPTSRGLFCPHQKLSQCHELWERNSYCKKVFVTCQDPNPAGLAAGTVASIILALVLLVVLLVVCGPLAYKKLVKKFRQKKQRQWIGPTGMNQNMSFHRNHTATVRSHAENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSMQPDNSSDSDYDLHGAQRL
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Molecular Weight
54.5 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
Leu recombinant proteins have emerged as a significant focus in the field of biotechnology and molecular biology due to their potential applications in various industries, including pharmaceuticals, agriculture, and nutrition. The study of Leu (leucine) recombinant proteins is mainly driven by the essential role that leucine plays in protein synthesis and muscle metabolism, making it crucial for health and development. Advances in genetic engineering techniques, such as CRISPR and plasmid-based expression systems, have facilitated the production of these proteins in model organisms, enhancing their availability and functionality. Furthermore, the investigation of Leu recombinant proteins contributes to our understanding of metabolic disorders and muscle wasting diseases, where leucine supplementation has shown promise in promoting muscle growth and recovery. The ability to engineer recombinant proteins with specific properties offers the potential for tailored therapeutic applications, making them a valuable subject of research. Consequently, the exploration of Leu recombinant proteins not only holds implications for enhancing agricultural productivity through improved crop resilience but also paves the way for developing innovative treatments for various health conditions linked to protein metabolism. This multifaceted approach underscores the relevance of Leu recombinant proteins in both scientific research and practical applications, highlighting the intersection of biochemistry, genetics, and health sciences.
