Cat: PA1000-4345

Recombinant Human CYGB Protein,His

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Analytical Data

  • Gene name

    CYGB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CYGB;STAP;Cytoglobin

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8WWM9

  • Expression Region

    1-190aa

  • AA Sequence

    MGSSHHHHHHSSGLVPRGSHMEKVPGEMEIERRERSEELSEAERKAVQAM WARLYASCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSPQLRK HACRVMGALNTVVENLHDPDKVSSVLALVGKAHALKHKVEPVYFKILSGV ILEVVAEEFASDFPPETQRAWAKLRGLIYSHVTAAYKEVGWVQQVPNATT PPATLPSSGP

  • Molecular Weight

    24 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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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.

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