Cathepsin B Polyclonal Antibody(Capture/Detector) (AN003800P)

For research use only.
Verified Samples | Verified Samples in ELISA: Recombinant Mouse Cathepsin B protein, Mouse serum, Mouse plasma, Rat serum, Rat plasma |
Dilution | ELISA Capture 2-8 μg/mL, ELISA Detector 0.1-0.4 μg/mL |
Isotype | Rabbit IgG |
Host | Rabbit |
Reactivity | Mouse, Rat |
Applications | ELISA Capture/Detector |
Clonality | Polyclonal |
Immunogen | Recombinant Mouse Cathepsin B Protein expressed by Mammalian |
Abbre | Cathepsin B |
Synonyms | Cathepsin B, Cathepsin B1, CB, Ctsb, APPS, CPSB |
Swissprot | |
Concentration | 1 mg/mL |
Buffer | Phosphate buffered solution, pH 7.2, containing 0.05% proclin 300. |
Purification Method | Antigen Affinity Purification |
Conjugation | Unconjugated |
Storage | Store at 4°C valid for 12 months or -20°C valid for long term storage, avoid freeze / thaw cycles. |
Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
background | 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. |
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