QF0159 Marketing Release Record

Primary Antibodies
Novocastra Tissue Inhibitor of Matrix
Metalloproteinase Antibodies
Clone 6F6a
1 mL lyophilized Tissue Inhibitor of Matrix
Metalloproteinase 1 NCL-TIMP1-485 P (HIER) W
Clone 46E5
1 mL lyophilized Tissue Inhibitor of Matrix
Metalloproteinase 2 NCL-TIMP2-487 P (HIER) W
Clone 18D12b
1 mL lyophilized Tissue Inhibitor of Matrix
Metalloproteinase 3 NCL-TIMP3 FP RUO*
The tissue inhibitors of metalloproteinases (TIMPs) are natural inhibitors of
matrix metalloproteinases (MMPs), a group of zinc-binding endopeptides
involved in degradation of the extracellular matrix (ECM). The remodelling of
the ECM in a controlled fashion is essential during normal development and
is a feature of physiological remodelling such as in wound healing. Tumor
cell invasion and metastasis closely correlate with the activities of two
MMPs, MMP2 and MMP9, both of which degrade type IV collagen in
basement membranes. TIMPs constitute a family of at least four types of
protein of which two of these are expressed in a wide variety of cell types.
Although TIMP2 inhibits all types of activated MMPs to varying degrees, it is
known to preferentially inhibit MMP2. TIMP2 also binds to proMMP9 and
proMMP2 to form stable complexes in which activation of the proenzymes
occur. Studies have revealed that TIMP2 can inhibit the invasive potential of
tumor cells in vitro and their metastatic phenotype in vivo. TIMP3 is secreted
into the ECM and complexes with MMP1, 3, 7, 9, 13, 14 and 15 deactivating
them irreversibly. TIMP3 mRNA is highly expressed in placenta but is also
reported to be found in the heart, kidney, lung, pancreas, uterus and skeletal
muscle with low levels in the brain. In early placenta, TIMP2 and TIMP3
mRNAs are reported to be found in cells of cytotrophoblastic columns and
decidual membrane. In endometrium, TIMP3 is reported to be expressed in
luminal epithelium, glands, stroma, endothelial cells and vascular smooth
muscle cells. In adult rat cerebellum, TIMP3 is reported to be expressed in
Purkinje cell somata and processes. TIMP3 is expressed by fibroblast-like
cells in ulcerated intestinal wall and in surrounding vessels and sweat
glands during wound healing in skin. In breast carcinoma, TIMP3 mRNA
expression is described in fibroblastic cells within the tumor stroma
adjacent to cancer cells.
Human small intestine: immunohistochemical staining for tissue inhibitor of matrix
metalloproteinase 1 using NCL-TIMP1-485. Note cytoplasmic staining of epithelial
cells. Paraffin section.
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RUO*
RUO*
Novocastra TNF-Related Apoptosis-
Inducing Ligand (TRAIL)
Clone 27B12
1 mL lyophilized NCL-TRAIL P (HIER) W
TRAIL (TNF-related apoptosis-inducing ligand), or APO-2L, is a 281 amino
acid cytotoxic protein closely related to Fas/APO-1 ligand with the
characteristic structure of a type II membrane protein. TRAIL induces
extensive apoptosis in lymphoid as well as nonlymphoid tumor cell lines.
Two TRAIL membrane receptors, DR4 and DR5, have been identified which
are capable of mediating apoptosis and are distinct from Fas/APO-1 and TNF
receptors. TRAIL-induced apoptosis in target cells is mediated by the
activation of caspases. Normal tissues are resistant to TRAIL as they are
reported to express high levels of decoy membrane receptors, DcR1/TRID
and DcR2/TRUNDD which antagonize TRAIL-induced apoptosis. TRAIL
induces apoptosis in a number of different tumor cell types because most
transformed cells express little DcR1. TRAIL mRNA is expressed in spleen,
lung, prostate, ovary and bowel with little expression in testis, heart, skeletal
muscle and pancreas. TRAIL protein is reported to be expressed on CD4 and
CD8 positive T lymphocytes following activation and is also predominant in
first trimester placental syncytiotrophoblasts as well as Hofbauer cells.
Human prostatic carcinoma: immunohistochemical staining for TNF-related apoptosisinducing
ligand using NCL-TRAIL. Note cytoplasmic staining of a proportion of malignant
cells. Paraffin section.
Novocastra Topoisomerase I
Clone 1D6
1 mL lyophilized NCL-TOPO I F P (HIER) Topoisomerases are
nuclear enzymes involved in a variety of cellular activities such as
chromosomal condensation, DNA replication, transcrip-tion, recombination
and segregation at mitosis. Human topoisomerase I is a 100 kD protein
capable of relaxing positively and negatively supercoiled DNA by performing
a transient single-stranded nick which is then re-ligated at the end of the
reaction. It has been shown that the enzyme is located in regions of the
genome that are undergoing active RNA synthesis where it probably
reduces superhelical stresses in the DNA enabling RNA polymerase to
function properly. In normal eukaryotic cells, DNA topoisomerase I does not
show relevant fluctuations across the cell cycle, unlike DNA topoisomerase
II alpha. Both DNA topoisomerases I and II have been found to be targets of
autoantibodies in the sera of individuals with certain autoimmune diseases
eg systemic lupus erythematosus and also of some anti-tumor drugs and
antibiotics. Elevated levels of DNA topoisomerase I, detected by 32 IVD
P transfer
assays, have been reported in colorectal tumors compared with normal
colon mucosa as a result of increased transcription or mRNA stability.
Product Specific Information
The use of phosphate-containing wash buffers or diluents with NCL-TOPO I
has an adverse effect on staining. Only Tris-containing wash buffers or
diluents should be used.
Products in this catalog are subject to regulatory approval.
Please consult your Leica Microsystems representative for availability in your region.
* For Research Use Only. Not for use in diagnostic procedures.
RUO*