QF0159 Marketing Release Record

Novocastra Caspase-9
Clone 2C9B11
1 mL, 0.1 mL lyophilized NCL-CASP-9 P (HIER) W
Caspase-9 is a member of the caspase family of cysteine proteases that has
been implicated in apoptosis and cytokine processing. Caspases have been
shown to be activated during normal human keratinocyte differentiation and
this activation is required for the normal loss of the nucleus. In addition, this
apoptotic pathway may be activated in cardiac myocytes under conditions
of ischemia. In the presence of ATP, apoptotic stimuli induce proteolytic
processing and activation of pro-caspase 9 by cytochrome c and Apaf-1.
Activated caspase-9 cleaves downstream caspases such as caspase-3, 6
and 7 initiating the caspase cascade. Caspase-9 is essential for apoptosis
during the normal development of the central nervous system. Mutations or
deficiencies in caspase-9 result in resistance to apoptotic stimuli that mimic
conditions in developing tumors.
Human rectal adenocarcinoma: immunohistochemical staining for caspase-9 protein using
NCL-CASP-9. Note cytoplasmic staining of neoplastic epithelium. Paraffin section.
Novocastra Cathepsin B
Clone CB131
1 mL lyophilized NCL-CATH-B P
RUO*
RUO*
Cathepsin B is one member of a family of proteolytic enzymes and is
expressed in cytoplasmic lysosomes in different types of normal and
neoplastic tissues. It is a cysteine protease and like most cathepsins is
involved in cellular metabolism such as protein degradation.
Immunohistochemical studies have detected expression in bowel mucosa,
skin, prostate and thyroid. Staining for cathepsin B, in common with other
cathepsins, may be so intense that it appears to be nuclear in some cells. A
proportion of endothelial cells are positive in many tissues. This has been
reported previously where it has been described as sprouting endothelial
cells. In tissues containing tumors this is thought to be related to tumor
progression. Cathepsin B is an important matrix-degrading protease in
several human cancers including lung adenocarcinomas, squamous cell
carcinomas, rectal and breast carcinomas. Cathepsin B is reported to be
overexpressed in squamous cell carcinoma where undifferentiated cells are
strongly positive and the more differentiated cells in tumor islands are either
weakly positive or negative. The expression of cathepsin B has also been
reported in melanomas where the upregulation of this enzyme was found to
be a characteristic of a more invasive tumor phenotype.
Human skin: immunohistochemical staining for cathepsin B using NCL-CATH-B. Note intense
cytoplasmic staining of basal epithelium and reduced staining in suprabasal cells. Paraffin
section.
Novocastra Cathepsin D
Clone C5
1 mL, 0.1 mL lyophilized NCL-CDm ASR
Analyte Specific Reagent. Analytical and performance characteristics are
not established.
Novocastra Cathepsin G
Clone 19C3
1 mL lyophilized NCL-CATH-G P (HIER) W
RUO*
Cathepsin G expression in normal tissues is restricted to granulocytes,
especially neutrophils. However, mononuclear phagocytes have been
demonstrated to bind and internalize proteases from neutrophils. Cathepsin
G is located in neutrophilic polymorphonuclear leukocytes which contain
specialized azurophil granules together with two other serine proteases;
elastase and hepsin. These three proteases may participate in the killing
and digestion of engulfed pathogens and in connective tissue remodelling at
sites of inflammation. Cathepsin G is also reported to be expressed in acute
and chronic myeloid leukemias whereas acute lymphoblastic or chronic
lymphocytic leukemias are negative for this protein.
Human tonsil: immunohistochemical staining for cathepsin G using NCL-CATH-G. Note intense
membrane staining of polymorphonuclear leukocytes. Paraffin section.
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
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Primary Antibodies