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CTSE Recombinant Protein

Source : Escherichia Coli. 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. Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinase expressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is an oncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variants encoding different isoforms exist for this gene.

Product Specifications

Product Name Alternative

Cathepsin E||EC 3.4.23.34||CATE||Erythrocyte Membrane Aspartic Proteinase||Slow-Moving Proteinase||EC 3.4.23.

Purification

"Greater than 85% as determined by SDS-PAGE."

Components

CTSE protein solution (1mg/mL) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Storage Conditions

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA) .Please avoid freeze thaw cycles.

Amino Acids

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
Curated Selection

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