C4618
Monoclonal Anti-Cathepsin L antibody produced in mouse
clone CPL33/1, purified from hybridoma cell culture
Synonym(s):
Anti-CATL, Anti-CTSL, Anti-MEP
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About This Item
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biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
CPL33/1, monoclonal
form
buffered aqueous solution
mol wt
antigen ~25 kDa (human cathepsin L)
antigen ~42 kDa (human pro cathepsin L)
species reactivity
human
concentration
~2 mg/mL
technique(s)
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: 0.1-0.2 μg/mL using total cell extracts of A549 cells
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CTSL1(1514)
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General description
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.
Specificity
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).
Application
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 Actions
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
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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Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
Cysteine cathepsins and the cutting edge of cancer invasion.
Gocheva V and Joyce J A
Cell Cycle, 6(1), 60-64 (2007)
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
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
Myung Jong Kim et al.
JCI insight, 9(3) (2024-02-08)
The glucocerebrosidase (GCase) encoded by the GBA1 gene hydrolyzes glucosylceramide (GluCer) to ceramide and glucose in lysosomes. Homozygous or compound heterozygous GBA1 mutations cause the lysosomal storage disease Gaucher disease (GD) due to severe loss of GCase activity. Loss-of-function variants
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