Human Cathepsin L Platinum ELISA

Also known as: Major excreted protein, MEP, Cathepsin L precursor

RUO: For Research Use Only. Not for use in diagnostic procedures.

SKU# BMS257*

Cat. No. Size
BMS257 96 tests
BMS257TEN 10 x 96 tests
Please inquire about custom configurations or bulk packaging.

To enable ordering, please select your country. Cookies will need to be enabled to continue on our website. View our Privacy Policy.

Data for Human Cathepsin L Platinum ELISA.

Click on image to view more information.

  • Data for Human Cathepsin L Platinum ELISA.
Description

Description: The human Cathepsin L ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human Cathepsin L. The human Cathepsin L ELISA is for research use only. Not for diagnostic or therapeutic procedures.

Cathepsin L is closely related to the recently described cathepsin V (L2) and the sequence indentity of almost 80% between them requires antibodies for the detection of cathepsin L which do not crossreact with cathepsin V. This requirement can only be met by epitope specific monoclonal antibodies as are used in BMS257.

Cathepsin L is a lysosomal cysteine proteinase consisting of a heavy chain of about 25 kDa and a light chain of about 5 kDa derived proteolytically from the same precursor. Cathepsin L has been shown to be produced by many different cell types. Since cathepsin L is capable of degrading protein constituents of the extracellular matrix it is assumed to play a crucial role in tumor progression and metastasis and a number of other disorders where the destruction of the extracellular matrix is the major cause of disease (e.g. rheumatoid arthritis, neurodegeneration).

Details
Reactivity Human
Sample Volume 50 uL
Suitable Sample Types cell culture supernatant, serum
Sensitivity 1.7 ng/mL
Standard Curve Range 3.1 - 50 ng/mL
Components Aluminium pouch(es) with a Microwell Plate coated with monoclonal antibody to human Cathepsin L
Biotin-Conjugate anti-human Cathepsin L monoclonal antibody
Streptavidin-HRP
Human Cathepsin L Standard lyophilized, 100 ng/ml upon reconstitution
Sample Diluent
Assay Buffer Concentrate 20x (PBS with 1% Tween 20 and 10% BSA)
Wash Buffer Concentrate 20x (PBS with 1% Tween 20)
Substrate Solution (tetramethyl-benzidine)
Stop Solution (1M Phosphoric acid)
Blue-Dye
Green-Dye
Red-Dye
Adhesive Films
Reported Applications ELISA
Documentation
TDS Link Download TDS
Related Products
Cat. No. Name Excite Emit Application Reg.
88-7004 CaspGLOW™ Fluorescein Active Caspase-3 Staining Kit FC, ICC RUO
BMS2016/2* Human MMP-9 Platinum ELISA ELISA RUO
BMS2070INST* Human EGF Instant ELISA ELISA RUO
BMS82018FF* Human TIMP-1 FlowCytomix Simplex Multiplex RUO
BMS500BT* Annexin V-Biotin Apoptosis Detection Kit FC RUO
References

References: Santamaria,I.; Velasco,G.; Pendas,A.M.; Paz,A.; Lopez-Otin,C.. Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J.Biol.Chem. 1999;274:13800-13809. (Link)

Mignatti,P.; Rifkin,D.B.. Biology and biochemistry of proteinases in tumor invasion. Physiol Rev. 1993;73:161-195. (Link)

Mason,R.W.; Massey,S.D.. Surface activation of pro-cathepsin L. Biochem.Biophys.Res.Commun. 1992;189:1659-1666. (Link)

Thomssen,C.; Oppelt,P.; Janicke,F.; Ulm,K.; Harbeck,N.; Hofler,H.; Kuhn,W.; Graeff,H.; Schmitt,M.. Identification of low-risk node-negative breast cancer patients by tumor biological factors PAI-1 and cathepsin L. Anticancer Res. 1998;18:2173-2180. (Link)

Taniguchi,S.; Nishimura,Y.; Takahashi,T.; Baba,T.; Kato,K.. Augmented excretion of procathepsin L of a fos-transferred highly metastatic rat cell line. Biochem.Biophys.Res.Commun. 1990;168:520-526. (Link)

Denhardt,D.T.; Greenberg,A.H.; Egan,S.E.; Hamilton,R.T.; Wright,J.A.. Cysteine proteinase cathepsin L expression correlates closely with the metastatic potential of H-ras-transformed murine fibroblasts. Oncogene 1987;2:55-59. (Link)

Keyszer,G.; Redlich,A.; Haupl,T.; Zacher,J.; Sparmann,M.; Engethum,U.; Gay,S.; Burmester,G.R.. Differential expression of cathepsins B and L compared with matrix metalloproteinases and their respective inhibitors in rheumatoid arthritis and osteoarthritis: a parallel investigation by semiquantitative reverse transcriptase-polymerase chain reaction and immunohistochemistry. Arthritis Rheum. 1998;41:1378-1387. (Link)

Tagami,K.; Kakegawa,H.; Kamioka,H.; Sumitani,K.; Kawata,T.; Lenarcic,B.; Turk,V.; Katunuma,N.. The mechanisms and regulation of procathepsin L secretion from osteoclasts in bone resorption. FEBS Lett. 1994;342:308-312. (Link)

Heidtmann,H.H.; Salge,U.; Havemann,K.; Kirschke,H.; Wiederanders,B.. Secretion of a latent, acid activatable cathepsin L precursor by human non-small cell lung cancer cell lines. Oncol.Res. 1993;5:441-451. (Link)

Flipo,R.M.; Heron,F.; Huet,G.; Balduyck,M.; Degand,P.; Duquesnoy,B.; Delcambre,B.. [Thiol-proteolytic activity in rheumatoid polyarthritis. Assay by spectrofluorimetry]. Rev.Rhum.Mal Osteoartic. 1991;58:131-133. (Link)

Chambers,A.F.; Colella,R.; Denhardt,D.T.; Wilson,S.M.. Increased expression of cathepsins L and B and decreased activity of their inhibitors in metastatic, ras-transformed NIH 3T3 cells. Mol.Carcinog. 1992;5:238-245. (Link)

Sivaparvathi,M.; Yamamoto,M.; Nicolson,G.L.; Gokaslan,Z.L.; Fuller,G.N.; Liotta,L.A.; Sawaya,R.; Rao,J.S.. Expression and immunohistochemical localization of cathepsin L during the progression of human gliomas 113. Clin.Exp.Metastasis 1996;14:27-34. (Link)

Santamaria,I.; Velasco,G.; Cazorla,M.; Fueyo,A.; Campo,E.; Lopez-Otin,C.. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res. 1998;58:1624-1630. (Link)

Kasai,M.; Shirasawa,T.; Kitamura,M.; Ishido,K.; Kominami,E.; Hirokawa,K.. Proenzyme from of cathepsin L produced by thymic epithelial cells promotes proliferation of immature thymocytes in the presence of IL-1, IL-7, and anti-CD3 antibody. Cell Immunol. 1993;150:124-136. (Link)

Yagel,S.; Warner,A.H.; Nellans,H.N.; Lala,P.K.; Waghorne,C.; Denhardt,D.T.. Suppression by cathepsin L inhibitors of the invasion of amnion membranes by murine cancer cells. Cancer Res. 1989;49:3553-3557. (Link)

Kim,K.; Cai,J.; Shuja,S.; Kuo,T.; Murnane,M.J.. Presence of activated ras correlates with increased cysteine proteinase activities in human colorectal carcinomas. Int.J.Cancer 1998;79:324-333. (Link)

Kolkhorst,V.; Sturzebecher,J.; Wiederanders,B.. Inhibition of tumour cell invasion by protease inhibitors: correlation with the protease profile. J.Cancer Res.Clin.Oncol. 1998;124:598-606. (Link)

Bromme,D.; Li,Z.; Barnes,M.; Mehler,E.. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 1999;38:2377-2385. (Link)

Xing,R.; Addington,A.K.; Mason,R.W.. Quantification of cathepsins B and L in cells. Biochem.J. 1998;332 ( Pt 2:499-505. (Link)

Cunnane,G.; FitzGerald,O.; Hummel,K.M.; Gay,R.E.; Gay,S.; Bresnihan,B.. Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis. Rheumatology.(Oxford) 1999;38:34-42. (Link)

Mason,R.W.; Johnson,D.A.; Barrett,A.J.; Chapman,H.A.. Elastinolytic activity of human cathepsin L. Biochem.J. 1986;233:925-927. (Link)

Chauhan,S.S.; Goldstein,L.J.; Gottesman,M.M.. Expression of cathepsin L in human tumors. Cancer Res. 1991;51:1478-1481. (Link)

Kakegawa,H.; Nikawa,T.; Tagami,K.; Kamioka,H.; Sumitani,K.; Kawata,T.; Drobnic-Kosorok,M.; Lenarcic,B.; Turk,V.; Katunuma,N.. Participation of cathepsin L on bone resorption 57. FEBS Lett. 1993;321:247-250. (Link)

Weber,E.; Gunther,D.; Laube,F.; Wiederanders,B.; Kirschke,H.. Hybridoma cells producing antibodies to cathepsin L have greatly reduced potential for tumour growth. J.Cancer Res.Clin.Oncol. 1994;120:564-567. (Link)

Pennacchio,L.A.; Lehesjoki,A.E.; Stone,N.E.; Willour,V.L.; Virtaneva,K.; Miao,J.; D'Amato,E.; Ramirez,L.; Faham,M.; Koskiniemi,M.; Warrington,J.A.; Norio,R.; de la,Chapelle A.; Cox,D.R.; Myers,R.M.. Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1) 97. Science 1996;271:1731-1734. (Link)


View More Products

AntigensArea of BiologyFormats