
- Species ReactivityHuman
- SpecificityDetects human Cathepsin L in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross‑reactivity with recombinant human Cathepsin B, C, L2, O, S, X/Z/P, or recombinant mouse Cathepsin H and L is observed.
- SourceMonoclonal Rat IgG2B Clone # 204106
- PurificationProtein A or G purified from hybridoma culture supernatant
- ImmunogenMouse myeloma cell line NS0-derived recombinant human Cathepsin L
Glu113-Val333
Accession # P07711 - FormulationLyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
- LabelUnconjugated
- Western Blot1 µg/mLSee below
- Immunohistochemistry8-25 µg/mLImmersion fixed paraffin-embedded sections of human kidney
- ReconstitutionReconstitute at 0.5 mg/mL in sterile PBS.
- ShippingThe product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
- Stability & StorageUse a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
- Goretzki, L. et al. (1992) FEBS Lett. 297:112.
- Taggart, C.C. et al. (2001) J. Biol. Chem. 276:33345.
- Gottesman, M.M. and F. Cabral (1981) Biochemistry 20:1659.
- Entrez Gene IDs:1514 (Human); 1514 (Human); 13039 (Mouse)
- Alternate Names:Cathepsin L; cathepsin L1; CATL; CTSL; CTSL1; CTSLEC 3.4.22.15; EC 3.4.22; FLJ31037; Major excreted protein; MEP
Background:
Cathepsin L is a lysosomal cysteine protease expressed in most eukaryotic cells. Cathepsin L is known to hydrolyze a number of proteins, including the proform of urokinase-type plasminogen activator, which is activated by Cathepsin L cleavage (1). Cathepsin L has also been shown to proteolytically inactivatealpha 1-antitrypsin and secretory leucoprotease inhibitor, two major protease inhibitors of the respiratory tract (2). These observations, combined with the demonstration of increased Cathepsin L activity in the epithelial lining fluid of the lungs of emphysema patients, have led to the suggestion that the enzyme may be involved in the progression of this disease. Cathepsin L has also been identified as a major excreted protein of transformed fibroblasts, indicating the enzyme could be involved in malignant tumor growth (3). 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.
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