Analytical Data
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Gene name
Rv1984c
- Application
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Alternative Names
Rv1984c；Carboxylesterase Culp1
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Species
E.coli
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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
P9WP43
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Expression Region
33-217aa
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AA Sequence
DPCSDIAVVFARGTHQASGLGDVGEAFVDSLTSQVGGRSIGVYAVNYPASDDYRASASNGSDDASAHIQRTVASCPNTRIVLGGYSQGATVIDLSTSAMPPAVADHVAAVALFGEPSSGFSSMLWGGGSLPTIGPLYSSKTINLCAPDDPICTGGGNIMAHVSYVQSGMTSQAATFAANRLDHAG
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Molecular Weight
38.7 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
The RV1984c protein, a recombinant protein derived from the bacterium *Rhodococcus sp.* strain RV1984, has garnered attention in recent years due to its potential applications in biotechnology and environmental remediation. This protein belongs to a class of enzymes known for their ability to degrade various organic compounds, including pollutants and xenobiotics. Research on RV1984c focuses on its biochemical properties, structural characteristics, and catalytic mechanisms, which can provide insights into its functionality and efficiency in breaking down complex substrates. The increasing prevalence of industrial waste and environmental contamination underscores the importance of developing effective bioremediation strategies, making RV1984c a promising candidate for such applications. Moreover, the exploration of RV1984c's genetic and protein engineering could lead to enhancements in its stability and activity, further expanding its utility in diverse fields, including pharmaceuticals, agriculture, and waste management. Understanding the distinct features and capabilities of RV1984c is crucial for harnessing its potential benefits in addressing critical environmental challenges.
