The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. The cysteine protease class comprises cathepsins B, L, H, K, S and O. The aspartyl protease class is composed of cathepsins D and E. Cathepsin G is in the serine protease class. Most cathepsins are lysosomal and each is involved in cellular metabolism, participating in various events such as peptide biosynthesis and protein degradation. Cathepsin L (also designated major excreted protein, MEP or CATL) is a member of the peptidase C1 family and has been identified as a protein that is most closely related to cathepsin H. Cathepsin L is a lysosomal cysteine proteinase that mediates intracellular protein catabolism for collagen, elastin and α-1 protease inhibitor. Cathepsin L is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene. Transformed mouse fibroblasts stimulated by growth factors or tumor promoters secrete a form of cathepsin L.

Cathepsin L1; Cathepsin L; Major excreted protein; MEP; Cathepsin L1 heavy chain; Cathepsin L1 light chain; CTSL; CTSL1

p07711

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 26 kDa

Rabbit

This antibody detects endogenous levels of Cathepsin L1 HC protein.

Synthetic peptide, corresponding to amino acids 230-288 of Human Cathepsin L1.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.