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Merck

C4618

Sigma-Aldrich

Monoclonal Anti-Cathepsin L antibody produced in mouse

clone CPL33/1, purified from hybridoma cell culture

Synonym(e):

Anti-CATL, Anti-CTSL, Anti-MEP

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

CPL33/1, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~25 kDa (human cathepsin L)
antigen ~42 kDa (human pro cathepsin L)

Speziesreaktivität

human

Konzentration

~2 mg/mL

Methode(n)

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: 0.1-0.2 μg/mL using total cell extracts of A549 cells

Isotyp

IgG1

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... CTSL1(1514)

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Allgemeine Beschreibung

Anti-Cathepsin L antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hybridoma CPL33/1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with human procathepsin L.
Monoclonal Anti-Cathepsin L (mouse IgG1 isotype) is derived from the hybridoma CPL33/1 produced by the fusion of mouse myeloma cells (P3X63Ag8.653) and splenocytes from BALB/c mice immunized with human procathepsin L.

Spezifität

The antibody recognizes the native and denaturated forms of the protein and does not cross react with human cathepsin V. Monoclonal Anti-Cathepsin L specifically recognizes human cathepsin L (∼ 25 kDa) and procathepsin L (∼ 42 kDa). Anti-Cathepsin L antibody epitope resides within amino acids of human cathepsin L (FYKE).

Immunogen

human procathepsin L. The antibody epitope resides within amino acids 258-261 of human cathepsin L (FYKE).

Anwendung

Anti-Cathepsin L antibody has been used for immunoblotting.
Monoclonal Anti-Cathepsin L antibody produced in mouse is suitable for:
  • immunohistochemistry
  • indirect ELISA
  • western blot : 0.1-0.2 μg/mL using total cell extracts of A549 cells

Biochem./physiol. Wirkung

Cathepsins are lysosomal proteases that play an important role in the intracellular degradation of exogenous and endogenous proteins, activation of enzyme precursors, and tumor invasion and metastasis.
Inhibition of the enzyme or the proenzyme by low molecular weight inhibitors or by specific antibodies led to a suppression of the invasive capabilities of malignant cells, or a decline in their ability to form tumors in experimental in vivo and in vitro models.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Cheuk-Yiu Law et al.
Biochemistry and biophysics reports, 5, 335-345 (2016-01-14)
Patients with Danon disease may suffer from severe cardiomyopathy, skeletal muscle dysfunction as well as varying degrees of mental retardation, in which the primary deficiency of lysosomal membrane-associated protein-2 (LAMP2) is considerably associated. Owing to the scarcity of human neurons
E Weber et al.
Hybridoma, 16(2), 159-166 (1997-04-01)
Mouse monoclonal antibodies directed against cathepsin L and procathepsin L have been generated. Mice were immunized with human procathepsin L purified from the cell culture medium of human nonsmall cell lung cancer cell line EPLC 32 M1. More than 400
Cysteine cathepsins and the cutting edge of cancer invasion.
Gocheva V and Joyce J A
Cell Cycle, 6(1), 60-64 (2007)
Boris Turk et al.
FEBS letters, 581(15), 2761-2767 (2007-06-05)
Proteases were, for a long time, mainly considered as protein degrading enzymes. However, in the last decade this view has changed dramatically, and the focus is now on proteases as signalling molecules. One of the best examples is apoptosis, the
S A Igdoura et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 43(5), 545-557 (1995-05-01)
Cathepsins are specific proteases in lysosomes that participate in the degradation of proteins, some of which are derived from endocytosis. In this study we examined the immunocytochemical localization of cathepsin B and D antibodies in cells of rat testis and

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