Analytical Data
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Gene name
CYGB
- Application
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Alternative Names
CYGB;STAP;Cytoglobin
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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
Q8WWM9
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Expression Region
1-190aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMEKVPGEMEIERRERSEELSEAERKAVQAM WARLYASCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSPQLRK HACRVMGALNTVVENLHDPDKVSSVLALVGKAHALKHKVEPVYFKILSGV ILEVVAEEFASDFPPETQRAWAKLRGLIYSHVTAAYKEVGWVQQVPNATT PPATLPSSGP
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Molecular Weight
24 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
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Protein Description
Cytochrome b561 (CYGB) is a heme-containing protein that plays a crucial role in electron transport and redox reactions within the cell, particularly in the context of mitochondrial and plasma membrane functions. Research into CYGB has gained traction due to its potential implications in various physiological processes, including oxidative stress response, cellular signaling, and oxygen regulation. Notably, CYGB's expression is observed in diverse tissues, suggesting its involvement in critical metabolic pathways. Studies have indicated that CYGB may participate in metabolic adaptation under hypoxic conditions and could be linked to various diseases, such as cancer and cardiovascular disorders. The recombinant expression of CYGB in model systems allows for the detailed study of its structural properties, functional mechanisms, and interactions with other cellular components. This research is not only fundamental for understanding CYGB's biological roles but also holds promise for therapeutic applications, such as gene therapy and the development of novel antioxidant strategies. As investigations continue to unravel the intricacies of CYGB, its role as a potential biomarker and therapeutic target in disease contexts is increasingly recognized, emphasizing the need for enhanced recombinant protein production techniques to facilitate further exploration.











