Analytical Data
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Gene name
RNLS
- Application
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Alternative Names
RNLS;C10orf59;Renalase
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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
Q5VYX0
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Expression Region
1-342aa
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AA Sequence
MAQVLIVGAGMTGSLCAALLRRQTSGPLYLAVWDKADDSGGRMTTACSPH NPQCTADLGAQYITCTPHYAKKHQRFYDELLAYGVLRPLSSPIEGMVMKE GDCNFVAPQGISSIIKHYLKESGAEVYFRHRVTQINLRDDKWEVSKQTGS PEQFDLIVLTMPVPEILQLQGDITTLISECQRQQLEAVSYSSRYALGLFY EAGTKIDVPWAGQYITSNPCIRFVSIDNKKRNIESSEIGPSLVIHTTVPF GVTYLEHSIEDVQELVFQQLENILPGLPQPIATKCQKWRHSQVTNAAANC PGQMTLHHKPFLACGGDGFTQSNFDGCITSALCVLEALKNYI
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Molecular Weight
64 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
Recombinant proteins have become essential in biotechnology and molecular biology due to their diverse applications in research, diagnostics, and therapeutics. RNLS (Ribonuclease-like protein) is a particular focus in this field, as it plays a critical role in various cellular processes, including RNA metabolism and regulation. The study of RNLS is significant for understanding its biological functions and potential therapeutic applications, particularly in cancer and viral infections where RNA regulation is crucial. The ability to produce RNLS as a recombinant protein allows researchers to investigate its structural properties, enzymatic activity, and interactions with other biomolecules. By employing advanced techniques such as genetic engineering, researchers can optimize the expression and purification of RNLS, leading to insights that can facilitate drug development and innovative treatment strategies. Furthermore, advancements in recombinant protein technology enable the creation of RNLS variants with tailored functionalities, enhancing its utility in various scientific and medical applications. This research contributes significantly to the growing body of knowledge surrounding RNA-related processes and the potential harnessing of RNLS for biotechnological innovations.
