Analytical Data
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Gene name
RCL
- Application
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Alternative Names
DNPH1;C6orf108;RCL;5-hydroxymethyl-dUMP N-hydrolase
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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
O43598
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Expression Region
1-174aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAAAMVPGRSESWERGEPGRPALYFCGSIR GGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQD LEWLQQADVVVAEVTQPSLGVGYELGRAVAFNKRILCLFRPQSGRVLSAM IRGAADGSRFQVWDYEEGEVEALLDRYFEADPPGQVAASPDPTT
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Molecular Weight
21 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
RCL (Rhodococcus, Clostridium, Lactobacillus) recombinant proteins have emerged as significant biological tools in various fields, particularly in biotechnology and medicine. The research background of RCL recombinant proteins is deeply rooted in the need for sustainable and efficient production of enzymes and bioactive compounds. With the increasing global demand for bioproducts, scientists have turned to microbial systems as an alternative to traditional chemical synthesis, leveraging the ability of these microorganisms to produce complex biomolecules. Rhodococcus, for instance, is known for its metabolic versatility and capability to degrade environmental pollutants, making it a valuable candidate for bioremediation applications. Clostridium species, on the other hand, are renowned for their ability to ferment diverse substrates and produce biofuels, while Lactobacillus is widely recognized for its probiotic properties and health benefits. By employing recombinant DNA technology, researchers can optimize the expression of specific genes from these organisms, resulting in the production of customized proteins with desired functionalities. This approach not only enhances yield and efficiency but also enables the tailoring of molecular properties for targeted applications, such as enzyme development, vaccine production, and therapeutic interventions. The ongoing exploration of RCL recombinant proteins is thus a pivotal aspect of contemporary scientific research, driven by the dual goals of advancing knowledge in microbial biotechnology and addressing pressing global challenges spanning health, environment, and sustainability.











