Recombinant Human CTSE Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0448NP
BL-0448NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0448NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human CTSE Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0448NP
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Product Overview

Description Recombinant Human Cathepsin E is produced by our Mammalian expression system and the target gene encoding Ser20-Pro396 is expressed with a 6His tag at the C-terminus.
Accession P14091
Synonym Cathepsin E; CTSE
Gene Background Cathepsin E (CTSE) is a gastric aspartyl protease that functions as a disulfide-linked homodimer. It is a member of the Peptidase C1 family, and has a specificity similar to that of Pepsin A and Cathepsin D. CTSE is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. It is expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. CTSE is an intracellular proteinase that have a role in immune function, activation-induced lymphocyte depletion in the thymus, neuronal degeneration and glial cell activation in the brain. Futhermore, it probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation.
Molecular Mass 41.78 KDa
Apmol Mass 46 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM MES, 150mM NaCl, pH 5.5.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target 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.
Subcellular Location Endosome. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.
Protein Families Peptidase A1 family
Database References
Tissue Specificity Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B-lymphocytes.

Gene Functions References

  1. Cathepsin E, mitochondrial fission, and caspase activation/apoptosis are linked in the pathogenesis of pulmonary emphysema. PMID: 25239563
  2. High Expression of Cathepsin E is associated with Tissues but Not Blood of Patients with Barrett's Esophagus and Adenocarcinoma. PMID: 25348778
  3. Decreased activity of cathepsin E produced by decidual macrophages might be responsible for the induction of miscarriages in some recurrent miscarriage patients. PMID: 24464956
  4. data demonstrate that CatE contributes to normal growth and development of mammary glands through proper trafficking and secretion of Wnt5a PMID: 24242330
  5. CTSE is a marker of both gastric differentiation and signet-ring cell carcinoma, which should shed light on the mechanism of gastric tumorigenesis. PMID: 23451082
  6. Cath E activity is useful as a potential molecular target for Pancreatic ductal adenocarcinoma and early detection imaging. PMID: 22068166
  7. A comparative structure model of splice variant 2 was computed based on its alignment to the known structure of cathepsin E intermediate (Protein Data Bank code 1TZS) and used to rationalize its conformational properties and loss of activity. PMID: 22718633
  8. Emerging roles of cathepsin E in immune system cells and skin keratinocytes, and in host defense against cancer cells. PMID: 21664991
  9. Cath E selectivity was established by having -Leu**Pro- residues at the scissile peptide bond. PMID: 20600629
  10. These results suggest the possible involvement of cathepsin E in disruption of the structural and functional integrity of alpha 2-macroglobulin in the endolysosome system. PMID: 12631277
  11. Reduced expression of cathepsin E is observed in erythrocytes of humans with atopic dermatitis. PMID: 14769879
  12. crystal structure of an activation intermediate of cathepsin E at 2.35A resolution PMID: 15342244
  13. Both cathepsin E message and protein are found in human dendritic cells, but are absent in monocytes. PMID: 15699105
  14. Three-dimensional structure of cathepsin-E. PMID: 15845357
  15. the human cathepsin E gene is regulated by the constitutive androstane receptor PMID: 17888866
  16. cathepsin E differentially regulates the nature and function of dendritic cells and macrophages PMID: 17947645
  17. cathepsin E plays a substantial role in host defense against tumor cells through TRAIL-dependent apoptosis and/or tumor-associated macrophage-mediated cytotoxicity PMID: 18006832
  18. CatE is important in the processing of tetanus toxin C-fragment in primary human B cells. PMID: 18996084
  19. This study demonstrates the over-expression in CTSE, in particular, and TFF1 in sessile serrated adenomas compared to both hyperplastic polyps and tubular adenomas. PMID: 19172291

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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