Rat Recombinant CTSE protein, His Tag (V2LY-0526-LY9200)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Rat
Tag
His Tag
Protein Construction
This product is Rat Recombinant CTSE protein, His Tag consist of Amino Acid: 1-398 and predicts a molecular mass of 42.1 kDa.
Molecule Mass
42.1 kDa
Sequence
Amino Acid: 1-398
Species
Rat

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>90% as determined by SDS-PAGE.
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
cathepsin E
Function
May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain.
Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB
Protein autoprocessing Source: Ensembl
Proteolysis Source: ARUK-UCL
Cellular Location
Endosome. The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.
PTM
Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide.
Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.

Zhu, Z., Wang, Q., Chen, X., Wang, Q., Yan, C., Zhao, X., ... & Zhu, W. H. (2022). An Enzyme‐Activatable Aggregation‐Induced‐Emission Probe: Intraoperative Pathological Fluorescent Diagnosis of Pancreatic Cancer via Specific Cathepsin E. Advanced Materials, 34(3), 2107444.

Wu, Y., Zhou, W., Yang, Z., Li, J., & Jin, Y. (2022). miR-185-5p Represses Cells Growth and Metastasis of Osteosarcoma via Targeting Cathepsin E. International Journal of Toxicology, 10915818211069270.

Kim, J. W., Cho, J. Y., Kim, J., Kim, D. G., Nam, B. H., Kim, Y. O., ... & Kong, H. J. (2020). First report of cathepsin E in a teleost (Korean rose bitterling, Rhodeus uyekii): Molecular characterisation and tissue distribution. Developmental & Comparative Immunology, 106, 103607.

Pontious, C., Kaul, S., Hong, M., Hart, P. A., Krishna, S. G., Lara, L. F., ... & Cruz-Monserrate, Z. (2019). Cathepsin E expression and activity: Role in the detection and treatment of pancreatic cancer. Pancreatology, 19(7), 951-956.

Hiramatsu, S., Watanabe, K. S., Zeggar, S., Asano, Y., Miyawaki, Y., Yamamura, Y., ... & Wada, J. (2019). Regulation of Cathepsin E gene expression by the transcription factor Kaiso in MRL/lpr mice derived CD4+ T cells. Scientific reports, 9(1), 1-13.

Mengwasser, J., Babes, L., Cordes, S., Mertlitz, S., Riesner, K., Shi, Y., ... & Penack, O. (2017). Cathepsin E deficiency ameliorates graft-versus-host disease and modifies dendritic cell motility. Frontiers in immunology, 8, 203.

Gonçalves, N. P., Moreira, J., Martins, D., Vieira, P., Obici, L., Merlini, G., ... & Saraiva, M. J. (2017). Differential expression of Cathepsin E in transthyretin amyloidosis: from neuropathology to the immune system. Journal of Neuroinflammation, 14(1), 1-12.

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For research use only. Not intended for any clinical use.

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