Analytical Data
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Gene name
rbcL
- Application
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Alternative Names
rbcL；Protein BUNDLE SHEATH DEFECTIVE 2. chloroplastic
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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
P0C512
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Expression Region
3-477aa
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AA Sequence
PQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRARGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIRSACKWSPELAAACEIWKAIKFEFEPVDKLDS
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Molecular Weight
60.1 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 rbcL gene encodes the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), a crucial enzyme in the process of photosynthesis. It is responsible for fixing carbon dioxide in the atmosphere, thereby playing a vital role in the carbon cycle and impacting global climate and plant productivity. Research on rbcL recombinant protein has garnered attention due to its potential applications in bioengineering, agriculture, and climate change mitigation. By expressing rbcL in different hosts, researchers aim to enhance the properties of RuBisCO, such as its efficiency and stability under varying environmental conditions. Furthermore, recombinant rbcL protein is instrumental in studying evolutionary relationships among plant species, as the gene is conserved across a wide range of plants. Understanding the variations in rbcL sequences can provide insights into plant evolution, adaptations, and responses to changing climates. Additionally, the exploration of rbcL as a biotechnological tool in carbon capture and sequestration is an emerging field that could contribute to sustainable agricultural practices and help address the challenges posed by climate change. Overall, the study of rbcL recombinant protein is significant for advancing our understanding of photosynthetic mechanisms, enhancing plant performance, and developing innovative solutions to environmental issues.
