Human Cathepsin L / CTSL1 Protein, His Tag

Source : 

Human Cathepsin L, His Tag (CT1-H5222) is expressed from human 293 cells (HEK293). It contains AA Thr 18 - Val 333 (Accession # NP_001903.1).

 

Molecule : Cathepsin L

 

Synonyms : CTSL1,MEP,CATL,CTSL

 

Format : Powder

 

Category : Bio-Markers & CD Antigens

 

Accession : NP_001903.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 25.0 kDa

 

Characteristics :

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 25.0 kDa. The protein migrates as 10 kDa and 34 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation, corresponding to the propeptide and the mature

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : 20 mM NaAc, 150 mM NaCl, pH5.0

 

Description :

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

 

References :

(1) Fujishima A., et al., 1997, FEBS Lett. 407:47-50.
(2) Goretzki L., et al., 1992, FEBS Lett, 297:112.
(3) Cailhier JF., et al., 2008, J. Biol. Chem., 283: 27220-27229.