Human Cathepsin L / CTSL1 Protein, Tag Free (Pro-form, HPLC verified)

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CAL-H5213-50ug
$367.00
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CAL-H5213-1mg
$2,205.00
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CAL-H5213
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Synonyms

CTSL1, MEP, CATL, CTSL

Source

Human Cathepsin L Protein, Tag Free (CAL-H5213) is expressed from human 293 cells (HEK293). It contains AA Thr 18 - Val 333 (Accession # P07711-1).

Predicted N-terminus: Thr 18

Molecular Characterization

This protein carries no "tag".

The protein has a calculated MW of 35.9 kDa. The protein migrates as 28-31 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

Purity

>90% as determined by SDS-PAGE.

>90% as determined by SEC-HPLC.

Formulation

Supplied as 0.2 μm filtered solution in 50 mM NaAC, 0.5 M NaCl, pH4.5 with glycerol as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.

Background

Cathepsin L (CTSL1) is also known as major excreted protein (MEP), is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains linked by disulfide bonds. CTSL1 is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. MEP has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. CTSL1 is important for the overall degradation of proteins in lysosomes. The specificity of MEP is close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z - Arg – Arg – NHMec, and no peptidyl - dipeptidase activity. Human Cathepsin L activity is greatest under mildly acidic conditions, from pH 4.5 ­ 6.5. The stability of the enzyme decreases at higher pH values