|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
Anti-CTSB rabbit polyclonal antibody at 1:500 dilution
Lane A: A549 Whole Cell Lysate
Lane B: HepG2 Whole Cell Lysate
Lane C: RAW264.7 Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:38 kDa
Observed band size:33 kDa
(We are unsure as to the identity of these extra bands.)
CTSB was immunoprecipitated using:
Lane A:0.5 mg HepG2 Whole Cell Lysate
Lane B:0.5 mg Raw264.7 Whole Cell Lysate
Lane C:0.5 mg A549 Whole Cell Lysate2 µL anti-CTSB rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-CTSB rabbit polyclonal antibody,at 1:200 dilutionSecondary antibody:
Dylight 800-labeled antibody to rabbit IgG (H+L), at 1:5000 dilutionDeveloped using the odssey technique.
Performed under reducing conditions.Predicted band size: 38 kDa
Observed band size: 38 kDa
Cathepsin B is a papain-family cysteine protease that is normally located in lysosomes, where it is involved in the turnover of proteins and plays various roles in maintaining the normal metabolism of cells. This protease has been implicated in pathological conditions, e.g., tumor progression and arthritis. In disease conditions, increases in the expression of cathepsin B occur at both the gene and protein levels. Cathepsin B is synthesized as a preproenzyme and the primary pathways for its normal trafficking to the lysosome utilize mannose 6-phosphate receptors (MPRs). Mature cathepsin B has the ability to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of several human and rodent tumors progression and arthritis. Cathepsin B expression is increased in many human cancers at the mRNA, protein and activity levels. It is also frequently overexpressed in premalignant lesions, an observation that associates this protease with local invasive stages of cancer. Increased expression of cathepsin B in primary cancers, and especially in preneoplastic lesions, suggests that this enzyme might have pro-apoptotic features. Active cathepsin B is also secreted from tumours, a mechanism likely to be facilitated by lysosomal exocytosis or extracellular processing by surface activators. Cathepsin B is localized to caveolae on the tumour surface, where binding to the annexin II heterotetramer occurs. Thus CTSB is suggested as a tumor marker. Additionally, Cathepsin B can degrade extracellular matrix proteins, such as collagen IV and laminin, and can activate the precursor form of urokinase plasminogen activator (uPA), perhaps thereby initiating an extracellular proteolytic cascade.
|Product Description||Host||Clonality||Application||Catalog# (PDF)|
|Anti-Cathepsin B Antibody||Rabbit||Polyclonal||ELISA||50084-RP01|
|Anti-Cathepsin B Antibody||Rabbit||Monoclonal||IHC-P||50084-R010|
|Anti-Cathepsin B Antibody||Rabbit||Polyclonal||ELISA||50084-T16|
|Anti-Cathepsin B Antibody||Rabbit||Monoclonal||ELISA||50084-R004|
|Anti-Cathepsin B Antibody||Rabbit||Polyclonal||ELISA||10483-RP01|
|Anti-Cathepsin B Antibody||Rabbit||Polyclonal||ELISA,IHC-P||10483-T24|
|Anti-Cathepsin B Antibody||Rabbit||Polyclonal||WB,ELISA,IHC-P||10483-T56|