Labelling Review row-Online

Primary Antibodies
Human pulmonary adenocarcinoma: immunohistochemical staining for thyroid transcription
factor-1 using NCL-TTF-1. Note nuclear staining in a proportion of tumor cells. Paraffin section.
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
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.
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Human small intestine: immunohistochemical staining for tissue inhibitor of matrix
metalloproteinase 1 using NCL-TIMP1-485. Note cytoplasmic staining of epithelial
cells. Paraffin section.
TNFR1-Associated Death Domain
Protein
Clone 18A11
1 mL lyophilized NCL-TRADD P (HIER)
TNFR1-Associated Death Domain Protein is also known as TRADD. Death
receptors of the TNF receptor family contain an intracellular death domain
that serves to recruit adaptor proteins such as TRADD and FADD and
cysteine proteases such as caspase-8. TRADD is a 34 kD protein containing
a death domain within its C-terminus which associates with the death
domain of TNFR1. Activation of TNFR1 or overexpression of TRADD induces
two opposite signalling pathways, caspase activation of apoptosis induction
and NF-kappaB activation for anti-apoptosis gene upregulation. Stat1
directly interacts with TNFR1 and TRADD, but not with FADD, and acts as a
TNFR1-signalling molecule to suppress NF-kappaB activation. TRADD is also
known to interact with the Epstein-Barr virus (EBV) latent membrane protein
1 (LMP1), the major oncogene of EBV. Human TRADD is reported to be
constitutively expressed at low levels in all tissues, while mouse TRADD
mRNA is expressed at higher levels in spleen, lung, liver and kidney and at
lower levels in brain, skeletal muscle and testis.
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.
Products in this catalog are subject to regulatory approval.
This catalog is not for use in the USA.