Human Cathepsin L / CTSL1 Protein, His Tag (active enzyme), Unconjugated 1 mg

Catalog Number: ABS-CAL-H52H3-1MG
Article Name: Human Cathepsin L / CTSL1 Protein, His Tag (active enzyme), Unconjugated 1 mg
Biozol Catalog Number: ABS-CAL-H52H3-1MG
Supplier Catalog Number: CAL-H52H3-1mg
Alternative Catalog Number: ABS-CAL-H52H3-1MG
Manufacturer: AcroBiosystems
Host: Human
Category: Proteine/Peptide
Species Reactivity: Human
Conjugation: Unconjugated
Cathepsin L (CTSL1) is also known as major excreted protein (MEP), is a member of the peptidase C1 family, is a dimer composed of disulfidelinked 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 alpha1 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 - Proteine/Peptide
Molecular Weight: 37.8 kDa
Tag: C-10*His
NCBI: 07711
Buffer: 50 mM NaAc, 0.5 M NaCl, pH4.5
Purity: 95%
Form: Liquid
Target: Cathepsin L
Immobilized Human Cathepsin L Protein, His Tag (Cat. No. CAL-H52H3) at 5 µg/mL (100 µL/well) can bind Human CD74, Fc Tag (Cat. No. CD4-H5256) with a linear range of 0.005-1.25 µg/mL (Routinely tested).
Human Cathepsin L Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.