Cathepsin L1 (CTSL1) Antikörper

Antigen: Cathepsin L1 (CTSL1)

Synonyme: MEP, CATL, CTSL, FLJ31037, fs, nkt, Ctsl1, 1190035F06Rik, Ctsl, CATHL, CTSL2, CTSL1, mep, catl, ctsl, cpl-1, MGC80629, MGC157400, MGC107932

Klonalität: Monoklonal (33-2)

Wirt: Maus

Reaktivität: Human, Maus, Ratte (Rattus)

Applikation: Immunhistochemie (Gefrierschnitte) (IHC (fro)), Enzyme Immunoassay (EIA), Western Blot (WB)

Produktnummer: ABIN151302

Produktbeschreibung

Weitere Bezeichnung: Cathepsin L1

Gen-ID: 1514, 13039, 25697

Immunogen: Purified full length native protein (Human lung cancer line EPLC 32 M1).

Format: Ascites

Isotyp: IgG1  (Passende Sekundärantikörper)

Klon: 33-2

Beschreibung: Cathepsins are lysosomal proteases that play an important role in the intracellulardegradation of exogenous and endogenous proteins, activation of enzyme precursors,and tumour invasion and metastasis. Normally located in lysosomes of almost allmammalian cells, they can be secreted from the cell under certain conditions. CathepsinL is responsible for most of the intralysosomal breakdown of normal cells. Cathepsin L issecreted by numerous transformed cells in its inactive proform, and mRNA expressionlevel seems to correlate with their metastatic potential. Alternate Names: anti-Cathepsin L heavy chain antibody, anti-Cathepsin L light chain antibody, anti-CATLantibody, anti-CTSL antibody, anti-Major excreted protein antibody, anti-MEP antibody.

Spezifität: Reacts specifically with the native and denatured forms of human cathepsin L (25kD)and procathepsin L (42 kD). Does not react with human cathepsin types B1, D1, H andS1, procathepsins B and D1 and recombinant procathepsin H, rat cathepsin B1, andmouse procathepsins B1 and D1. Species Reactivity: Cross-reacts with Human, Mouse procathepsin L (weak), Rat cathepsin L (strong), andMink cathepsin and procathepsin L. Not yet tested in other species. Localization: Lysosomes.

Anwendungen

Applikationshinweise: Suggested working dilutions: Western Blot 1/200, Positive Controls: Whole cell extract from cultured mink lung cell line.

Konzentration: 4.8 mg/ml

Buffer: Preservative: 15 mM sodium Azide.

Lagerung: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze thaw cycles.

Forschungsgebiet: Proteasen, Krebs

Beschränkungen: Nur für Forschungszwecke einsetzbar

Publikationen

Publikationen: Trabandt, Aicher, Gay et al.: "Expression of the collagenolytic and Ras-induced cysteine proteinase cathepsin L and proliferation-associated oncogenes in synovial cells of MRL/I mice and patients with rheumatoid arthritis." in: Matrix (Stuttgart, Germany), Vol. 10, Issue 6, pp. 349-61, 1991 (PubMed).

Bellelli, Mattioni, Rusconi et al.: "Inhibition of tumor growth, invasion and metastasis in papain-immunized mice." in: Invasion & metastasis, Vol. 10, Issue 3, pp. 142-69, 1990 (PubMed).

Yamaguchi, Chung, Shiroeda et al.: "Characterization of a cathepsin L-like enzyme secreted from human pancreatic cancer cell line HPC-YP." in: Cancer research, Vol. 50, Issue 3, pp. 658-63, 1990 (PubMed).

Igdoura, Morales, Hermo: "Differential expression of cathepsins B and D in testis and epididymis of adult rats." in: The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, Vol. 43, Issue 5, pp. 545-57, 1995 (PubMed).

Weber, Guenther, Laube et al.: "Hybridoma cells producing antibodies to cathepsin L have greatly reduced potential for tumour growth." in: Journal of cancer research and clinical oncology, Vol. 120, Issue 9, pp. 564-7, 1994 (PubMed).

Heidtmann, Salge, Havemann et al.: "Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines." in: Oncology research, Vol. 5, Issue 10-11, pp. 441-51, 1994 (PubMed).

Mignatti, Rifkin: "Biology and biochemistry of proteinases in tumor invasion." in: Physiological reviews, Vol. 73, Issue 1, pp. 161-95, 1993 (PubMed).

Sivaparvathi, Yamamoto, Nicolson et al.: "Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas." in: Clinical & experimental metastasis, Vol. 14, Issue 1, pp. 27-34, 1996 (PubMed).

Zheng, Chou, Mirkin et al.: "Senescence-initiated reversal of drug resistance: specific role of cathepsin L." in: Cancer research, Vol. 64, Issue 5, pp. 1773-80, 2004 (PubMed).

Zheng, Chu, Chou et al.: "Cathepsin L inhibition suppresses drug resistance in vitro and in vivo: a putative mechanism." in: American journal of physiology. Cell physiology, Vol. 296, Issue 1, pp. C65-74, 2009 (PubMed).