QF0159 Marketing Release Record

Novocastra Folylpolyglutamate
Synthetase
Clone AS2
1 mL, 0.1 mL liquid NCL-L-FPGS P (HIER)
Antigen Background
Folic acid is a water soluble vitamin, essential for normal cell growth and
replication. Eukaryotes, however are unable to synthesize folates and
therefore require an external source. Following uptake by the cell, folates are
retained within the cell by polyglutamation, catalyzed by folylpolyglutamate
synthetase (FPGS). Folates act as carriers of one carbon units, which are vital
for the biosynthesis of purines, thymidylate and hence DNA replication.
Polyglutamation by FPGS increases binding of folate co-factors to enzymes of
folate biosynthesis, prevents efflux of folate co-factors from the cell and
allows the accumulation of folates required for glycine synthesis in the
mitochondria. FPGS also plays an important role in the cellular retention of
folate analogs/antifolates and is reported to play a role in the selective
cytotoxicity of such compounds used for the treatment of human cancers.
Human adrenal medulla: immunohistochemical staining for folypolyglutamate synthesase
(FPGS) using NCL-L-FPGS. Paraffin section.
Novocastra Galectin-1
Clone 25C1
1 mL, 0.1 mL lyophilized NCL-GAL1 P (HIER) W
Galectin-1 is a member of the beta-galactoside-binding family and is a
pleiotropic dimeric protein of 14 kD participating in a variety of normal and
pathological processes, including cancer progression. Galectin-1 can affect
the proliferation of normal and malignant cells. Inhibition of cell growth is
observed in a lactose-dependent manner as lower concentrations of the
lectin stimulate cell proliferation. Galectin-1 may also be implicated in the
induction of apoptosis of activated T cells through the binding of exogenous
galectin-1 to CD45 molecules present on the surface of lymphocytes.
Galectin-1, reported to be present either at the surface of cancer cells or
accumulated around these cells could act as an immunological shield to
protect against a T cell immune response and provide an advantage for
survival. Galectin-1 is reported to be expressed by a variety of malignant
tumors including thyroid carcinoma. In colon carcinomas, the progressive
overexpression of galectin-1 has been reported to be demonstrated during
the evolution from normal to malignant cell type. Galectin-1 has not been
detected in the cells of normal prostate, prostatic intra-epithelial neoplasia
or prostatic carcinoma cells. However, galectin-1 is reported to be
detectable in the stroma and associated fibroblasts of these tissues and is
significantly increased in the tumor-associated stroma compared with nonneoplastic
gland-associated stroma in a proportion of these. Three laminin
binding proteins, galectin-1 together with galectin-3 and laminin receptor
have been shown to effect similar qualitative and quantitative cell surface
changes in cancer cells allowing them to cross basement membranes
during metastatic spread. These changes in expression are reported in
breast, colon, ovarian and uterine cancers.
IVD
RUO*
Normal human prostate: immunohistochemical staining for Galectin-1 using NCL-GAL1.
Note staining in the stroma and cytoplasmic staining of fibroblasts. Paraffin section.
Novocastra Galectin-3
Clone 9C4
1 mL, 0.1 mL lyophilized NCL-GAL3 P (HIER) W
7 mL BOND ready-to-use PA0238 P (HIER) IVD
Antigen Background
Galectin-3 is a member of the beta-galactosidase-binding lectin family. It is
involved in several biological events including binding to the basement
membrane glycoprotein laminin. Cell surface galectin-3 may be involved in
homotypical cell adhesion and is downregulated in colon cancer as the
disease progresses. This downregulation has also been examined in breast
carcinoma with a similar correlation of expression reported. Downregulation
of galectin-3 could be one of the many events that enable cancer cells to
interact with laminin to facilitate invasion and metastasis and may indicate
activation of the invasive phenotype in various tumor types. Galectin-3 has
been reported to be detected in anaplastic large cell lymphomas, whereas
galectin-3 is not detected in Reed Sternberg cells or variants of Hodgkin's
disease.
Novocastra Gamma-Catenin
Clone 11B6
1 mL lyophilized NCL-G-CAT F P (HIER) W
RUO*
Cell to cell adhesion is mediated by cadherins which form a complex with
catenins. Gamma-catenin or plakoglobin, is a major cytoplasmic protein of
82 kD that occurs in soluble and membrane-associated forms. The downregulation
of cadherins and catenins has been detected in many types of
human carcinomas and has been reported to be associated with tumor
progression. E-cadherin and the catenins are reported to be expressed in
normal epithelium as well as urothelium. E-cadherin plays a primary role in
the maintenance of epithelial integrity where its decrease or loss of
expression is reported to be strictly associated with neoplastic progression
in a variety of human carcinomas, including bladder carcinoma. The
combined decrease in expression of gamma-catenin, beta-catenin and Ecadherin
is found at the invasive front of both grade 2 and some grade 1
carcinomas, further supporting a link with the aggressive behavior of those
cancer cells. In thyroid carcinomas, catenins are also reported to be
downregulated at cell to cell junctions. Gamma-catenin expression is
reported to be partially or totally lost in the majority of papillary, follicular
and anaplastic thyroid carcinomas.
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
IVD
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Primary Antibodies