Labelling Review row-Online

Primary Antibodies
Folate Receptor Alpha
Clone BN3.2 New!
1 mL, 0.1 mL liquid NCL-L-FRalpha P (HIER)
Folate is a basic component of cell metabolism and DNA synthesis and
repair. It is involved in essential one-carbon transfer reactions and is a
vitamin required by both normal and tumor cells. Folate entry into cells is
facilitated via two different systems: the reduced folate carrier, which
utilizes a bidirectional anion-exchange mechanism, and the folate receptor
system. Folate receptor alpha is a membrane–bound member of the folate
receptor family, facilitating folate transport via a mechanism termed
potocytosis where the receptor is internalized and then recycled back to the
cell membrane. Staining patterns are both membrane and cytoplasmic due
to this mechanism. Members of the folate receptor family share highly
conserved sequences in the open reading frames, but differ in amino acids
in the 5’ untranslated regions and as a consequence can differ in function
and tissue expression. Folate receptor alpha expression is reported to be
highly restricted in normal tissues and only selectively overexpressed in a
limited number of epithelial malignancies.
Ovarian tumor: immunohistochemical staining for Folate Receptor Alpha using NCL-L-FRalpha.
Note intense cytoplasmic staining. Paraffin section.
Folylpolyglutamate Synthetase
Clone AS2 New!
1 mL, 0.1 mL liquid NCL-L-FPGS P (HIER)
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 cofactors
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.
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Reference Range
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.
Normal human prostate: immunohistochemical staining for Galectin-1 using NCL-GAL1.
Note staining in the stroma and cytoplasmic staining of fibroblasts. Paraffin section.
Galectin-3
Clone 9C4
1 mL, 0.1 mL lyophilized NCL-GAL3 P (HIER) W
7 mL Bond ready-to-use PA0238 P (HIER) New!
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.
Refer to page 29 for the Bond ready-to-use format.
Products in this catalog are subject to regulatory approval.
This catalog is not for use in the USA.