Analytical Data
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Gene name
CYBA
- Application
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Alternative Names
CYBACytochrome b-245 light chain; Cytochrome b(558) alpha chain; Cytochrome b558 subunit alpha; Neutrophil cytochrome b 22 kDa polypeptide; Superoxide-generating NADPH oxidase light chain subunit; p22 phagocyte B-cytochrome; p22-phox; p22phox
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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
P13498
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Expression Region
2-195aa
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AA Sequence
GQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVFVC LLEYPRGKRK KGSTMERWGQ KYMTAVVKLF GPFTRNYYVR AVLHLLLSVP AGFLLATILG TACLAIASGI YLLAAVRGEQ WTPIEPKPRE RPQIGGTIKQ PPSNPPPRPP AEARKKPSEE EAAVAAGGPP GGPQVNPIPV TDEVV
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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
CYBA, also known as cytochrome b-245 alpha chain, plays a crucial role in the functioning of the NADPH oxidase complex, which is essential for generating reactive oxygen species (ROS) involved in various physiological processes and immune responses. Research into the recombinant form of CYBA protein has gained traction due to its importance in understanding oxidative stress-related diseases, such as chronic inflammation, cardiovascular disorders, and neurodegenerative diseases. The recombinant CYBA protein allows for detailed studies of its structure-function relationships and interaction with other subunits of the NADPH oxidase complex. Furthermore, the expression and purification of CYBA in suitable systems enable the investigation of its enzymatic mechanisms and the modulation of ROS production. Advances in recombinant technology have facilitated the large-scale production of CYBA, paving the way for drug discovery and the development of therapeutic interventions targeting oxidative stress pathways. Investigating the properties and functions of CYBA through recombinant protein studies could ultimately lead to novel strategies for managing diseases associated with dysregulated ROS levels, highlighting the significance of this research in biomedical science.
