Recombinant Cricetulus griseus Peroxiredoxin-1 (PRDX1)

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Code CSB-YP872876DXU
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Size $436
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  • Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of CSB-YP872876DXU could indicate that this peptide derived from Yeast-expressed Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) PRDX1.
  • Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of CSB-YP872876DXU could indicate that this peptide derived from Yeast-expressed Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) PRDX1.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Cardiovascular
Alternative Names
PRDX1; TDPX2Peroxiredoxin-1; EC 1.11.1.15; Thioredoxin peroxidase 2; TPX-2
Species
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Source
Yeast
Expression Region
2-199aa
Target Protein Sequence
SSGNAKIGYPAPNFKATAVMPDGQFRDICLSEYRGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEILRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
24.2 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
Tris-based buffer,50% glycerol
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The recombinant Cricetulus griseus Peroxiredoxin-1 (PRDX1) is produced by manipulating the expression of specific genes in yeast cells. The gene fragment encoding the Cricetulus griseus PRDX1 protein (2-199aa) is fused to an expression vector along with the N-terminal 6xHis-tag gene and subsequently transformed into yeast cells. The cells that successfully integrate the vector are selected and cultured to induce the expression of the desired protein. The recombinant Cricetulus griseus PRDX1 protein is then purified using affinity purification, achieving a purity level of over 90%, as confirmed by SDS-PAGE analysis.

PRDX1 is a multifunctional protein that acts as a hydrogen peroxide scavenger, a molecular chaperone, and an immune modulator [1]. PRDX1 protects cells from oxidative stress by scavenging oxidants and regulating reactive oxygen species [2][3]. PRDX1 is also involved in different types of cancers, such as breast cancer, colorectal cancer, esophageal cancer, osteosarcoma, head and neck squamous cell carcinoma, and renal cell carcinoma [1][4][2][5][6][7]. In breast cancer, PRDX1 has been identified as a protein biomarker associated with a favorable prognosis [1].

PRDX1 regulates various cellular processes, including cell growth, differentiation, apoptosis, and metastasis [1][8][5][6]. PRDX1 promotes the proliferation and metastasis of cancer cells by enhancing the Akt/mTOR pathway [5]. Additionally, PRDX1 can drive cancer progression by inhibiting ferroptosis and suppressing NRF2 degradation [4]. In esophageal squamous cell carcinoma, PRDX1 causes primary cilia loss, leading to tumor formation [9].

It has been demonstrated that PRDX1 inhibits tumorigenesis by modulating PTEN/AKT signaling pathways [10]. Additionally, PRDX1 has been associated with endothelial activation and early atherosclerosis, suggesting its involvement in vascular health [11].

References:
[1] P. O’Leary, M. Terrile, M. Bajor, P. Gaj, B. Hennessy, G. Millset al., Peroxiredoxin-1 protects estrogen receptor α from oxidative stress-induced suppression and is a protein biomarker of favorable prognosis in breast cancer, Breast Cancer Research, vol. 16, no. 4, 2014. https://doi.org/10.1186/bcr3691
[2] Y. Song, H. Liu, C. Cui, X. Peng, C. Wang, X. Tianet al., <p>silencing of peroxiredoxin 1 inhibits the proliferation of esophageal cancer cells and promotes apoptosis by inhibiting the activity of the pi3k/akt pathway</p>, Cancer Management and Research, vol. Volume 11, p. 10883-10890, 2019. https://doi.org/10.2147/cmar.s235317
[3] J. Robles, Integrated meta-analysis of colorectal cancer public proteomic datasets for biomarker discovery and validation, Plos Computational Biology, vol. 20, no. 1, p. e1011828, 2024. https://doi.org/10.1371/journal.pcbi.1011828
[4] X. Yu, Prdx1 drives colorectal cancer progression by inhibiting ferroptosis through suppression of cullin-3-mediated nrf2 degradation,, 2024. https://doi.org/10.21203/rs.3.rs-4242780/v1
[5] A. Cai, W. Zeng, W. Cai, J. Liu, X. Zheng, Y. Liuet al., Peroxiredoxin-1 promotes cell proliferation and metastasis through enhancing akt/mtor in human osteosarcoma cells, Oncotarget, vol. 9, no. 9, p. 8290-8302, 2017. https://doi.org/10.18632/oncotarget.23662
[6] Y. Jiang, W. Cao, K. Wu, X. Qin, X. Wang, Y. Liet al., Lncrna linc00460 promotes emt in head and neck squamous cell carcinoma by facilitating peroxiredoxin-1 into the nucleus, Journal of Experimental & Clinical Cancer Research, vol. 38, no. 1, 2019. https://doi.org/10.1186/s13046-019-1364-z
[7] X. Zhou, Z. Liang, K. Li, W. Fang, Y. Tian, X. Luoet al., Exploring the natural piericidins as anti-renal cell carcinoma agents targeting peroxiredoxin 1, Journal of Medicinal Chemistry, vol. 62, no. 15, p. 7058-7069, 2019. https://doi.org/10.1021/acs.jmedchem.9b00598
[8] C. Ding, X. Fan, & G. Wu, Peroxiredoxin 1 – an antioxidant enzyme in cancer, Journal of Cellular and Molecular Medicine, vol. 21, no. 1, p. 193-202, 2016. https://doi.org/10.1111/jcmm.12955
[9] Q. Chen, J. Li, X. Yang, J. Ma, F. Gong, & Y. Liu, Prdx1 promotes the loss of primary cilia in esophageal squamous cell carcinoma,, 2020. https://doi.org/10.21203/rs.2.17849/v2
[10] J. Cao, J. Schulte, B. Knight, N. Leslie, A. Zagożdżon, R. Bronsonet al., Prdx1 inhibits tumorigenesis via regulating pten/akt activity, The Embo Journal, vol. 28, no. 10, p. 1505-1517, 2009. https://doi.org/10.1038/emboj.2009.101
[11] J. Kisucka, A. Chauhan, I. Patten, A. Yesilaltay, C. Neumann, R. Ettenet al., Peroxiredoxin1 prevents excessive endothelial activation and early atherosclerosis, Circulation Research, vol. 103, no. 6, p. 598-605, 2008. https://doi.org/10.1161/circresaha.108.174870

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Target Background

Function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation.
Subcellular Location
Cytoplasm.
Protein Families
Peroxiredoxin family, AhpC/Prx1 subfamily
Database Links
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