Analytical Data
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Gene name
catA
- Application
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Alternative Names
catA；Catalase
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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
P07773
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Expression Region
1-311aa
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AA Sequence
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV
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Molecular Weight
50.3 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
CatA, a crucial member of the catalase family, functions as an antioxidant enzyme that decomposes hydrogen peroxide into water and oxygen, thus protecting cells from oxidative stress. Research on CatA has gained increasing prominence due to its potential implications in various biological processes and diseases, including aging, neurodegeneration, and inflammation. The study of recombinant CatA proteins has advanced our understanding of its structural and functional properties, enabling the exploration of its catalytic mechanisms and regulatory pathways. Advances in molecular cloning and protein expression techniques have allowed scientists to produce large quantities of pure, active CatA, facilitating detailed biochemical analyses. Moreover, the recombinant form of CatA holds promise for therapeutic applications, such as in the development of antioxidant treatments that could mitigate oxidative damage in disease contexts. As researchers continue to investigate the various roles of CatA in cellular defense mechanisms, the potential for engineering CatA variants with enhanced activity or stability opens new avenues for biotechnology and pharmaceutical development. Therefore, elucidating the characteristics and applications of CatA recombinant proteins remains a pivotal area of study in the broader context of redox biology and therapeutic innovation.
