CTSE Human
Cathepsin-E Human Recombinant
Cat. No.
BT30527
Source
Escherichia Coli.
Synonyms
Cathepsin
E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving
Proteinase, EC 3.4.23.
Appearance
Sterile Filtered clear solution.
Purity
Greater
than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
CTSE Human Recombinant produced in E.Coli is a single,
non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and
having a molecular mass of 35.4kDa.
CTSE is fused to a 23 amino acid His-tag at
N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Cathepsin-E, also known as CTSE, is a gastric aspartyl protease that functions as a disulfide-linked homodimer. It belongs to the peptidase C1 family and exhibits specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase primarily found in the surface of epithelial mucus-producing cells of the stomach. It is not believed to be involved in dietary protein digestion. Notably, CTSE is the first aspartic proteinase expressed in the fetal stomach and is found in over half of gastric cancers, making it an oncofetal antigen. Multiple transcript variants exist for this gene, including those utilizing alternative polyadenylation signals and those encoding different isoforms.
Description
Recombinant human CTSE, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 330 amino acids (residues 57-363). It has a molecular mass of 35.4 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
CTSE protein solution at a concentration of 1 mg/ml in 20 mM Tris-HCl buffer (pH 8.0), 0.4 M urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For longer storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity greater than 85% as determined by SDS-PAGE analysis.
Synonyms
Cathepsin
E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving
Proteinase, EC 3.4.23.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW
VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG
QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM
LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ
SLTVGITVWD WPQQSPKEGP CVCACLSDRP
Product Science Overview
Cellular Distribution and Function
Challenges in Isolation
Recombinant Production
Applications in Research
Recombinant Cathepsin-E is used in studies related to its role in antigen processing, biogenesis of endothelin, and its involvement in HIV infection . It is also used in assays to measure its enzymatic activity, which is crucial for understanding its function and potential therapeutic applications .
Cathepsin-E continues to be a subject of interest due to its unique properties and potential implications in various physiological and pathological processes.
Quick Inquiry
Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
