Labelling Review row-Online

Primary Antibodies
Caspase-8
Clone 11B6
1 mL, 0.1 mL lyophilized NCL-CASP-8 F P (HIER)
The caspases represent a family of cysteine proteases that play important
regulatory roles within the cell. Caspase-8, also called FLICE, has an Nterminal
domain with sequence homology to the death effector domain of
FADD that allows association of caspase-8 with the TNF/Fas family of
receptors. This association with the cell surface death receptors has shown
caspase-8 to be a proximal regulator of apoptosis. Caspase-8 is activated by
association with the Fas/FADD death-inducing signalling complex to release
two active subunits, p18 and p10, into the cytosol, where they activate other
caspases amplifying the apoptotic signal. Caspase-8 is reported to be
expressed in pancreatic tumors, high grade non-Hodgkin's lymphomas and
invasive breast carcinomas.
Product Specific Information
NCL-CASP-8 is raised to the p18 subunit found in caspases 8a, 8b and 8h.
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.
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Cathepsin B
Clone CB131
1 mL lyophilized NCL-CATH-B P
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.
Cathepsin D
Clone C5
1 mL, 0.1 mL lyophilized NCL-CDm FP
Cathepsins are members of the papain family of cysteine lysosomal
proteases which are involved in a variety of physiological processes such
as proenzyme activation, enzyme inactivation, antigen presentation,
hormone maturation, tissue remodelling and bone matrix resorption.
Cathepsin D is first produced in a precursor form, pro-cathepsin D (52 kD),
and then processed in the cell to an intermediate form of 48 kD, then finally
to the mature forms of 34 kD and 14 kD. It has been proposed that the
presence of high levels of cathepsin D in breast cancer may signify a
functional estrogen receptor apparatus.
Human breast carcinoma: immunohistochemical staining for cathepsin D using NCL-CDm.
Note granular cytoplasmic staining of tumor cells. Paraffin section.
Products in this catalog are subject to regulatory approval.
This catalog is not for use in the USA.