Recombinant Human Cathepsin E (CTSE) (Active)

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Code CSB-AP005661HU
Size $290
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU/μg as determined by LAL method.
Activity
Specific activity as determined by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 is greater than 1500 pmol/min/ug
Target Names
CTSE
Uniprot No.
Research Area
Cancer
Alternative Names
CATE; CATE_HUMAN; Cathepsin E; Cathepsin E form II; CTSE; Erythrocyte membrane aspartic proteinase ; Slow moving proteinase
Species
Homo sapiens (Human)
Source
Mammalian cell
Expression Region
20-396aa
Complete Sequence
SLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP
Mol. Weight
41.78 kDa
Protein Length
Full Length of Mature Protein
Tag Info
C-terminal 6xHis-tagged
Form
Lyophilized powder
Buffer
Lyophilized from a 0.2 μm Filtered 20 mM MES, 150 mM NaCl, pH 5.5
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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
Basically, we can dispatch the products out in 5-10 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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

Our Recombinant Human CTSE protein is an essential research tool for scientists in the field of cancer biology. Cathepsin E, also known as CTSE, is produced in mammalian cells and features the full-length expression region from 20-396aa. The protein is fused with a C-terminal 6xHis-tag for ease of purification and identification. The lyophilized powder format allows for straightforward reconstitution with sterile water or buffer to suit various experimental needs.

The Recombinant Human CTSE protein demonstrates high quality and performance with a purity greater than 95%, as determined by SDS-PAGE analysis. Additionally, endotoxin levels are maintained below 1.0 EU/µg, as assessed by the LAL method. The protein exhibits specific activity greater than 1500 pmol/min/ug, as determined by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2, highlighting its functionality for relevant applications.

Human CTSE has been a subject of interest in numerous research studies due to its role in the degradation of intracellular proteins and its implications in cancer biology. Research conducted by Chain et al. (2005)[1] and Vidak et al. (2017)[2] contributed to a better understanding of the function and potential clinical applications of CTSE. These studies highlight the importance of CTSE in tumorigenesis, tumor progression, and its potential therapeutic value in cancer treatment.

References:
1. Chain BM, et al. The expression and function of cathepsin E in dendritic cells. J Immunol. 2005;174(4):1791-800.
2. Vidak E, et al. The role of cathepsin E in normal and pathological processes. Exp Biol Med (Maywood). 2017;242(10):1043-53.

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Target Background

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.
Gene References into Functions
  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

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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
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.
Database Links

HGNC: 2530

OMIM: 116890

KEGG: hsa:1510

STRING: 9606.ENSP00000350911

UniGene: Hs.644082

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