Labelling Review row-Online

Human appendix: immunohistochemical staining for mast cell tryptase using NCL-MCTRYP-
428. Note cytoplasmic staining of mast cells. Paraffin section.
Matrix Metalloproteinase Antibodies
Clone 17B11
1 mL, 0.1 mL lyophilized Matrix Metalloproteinase 2
NCL-MMP2-507 P (HIER)
Clone 15W2
1 mL, 0.1 mL lyophilized Matrix Metalloproteinase 9
NCL-MMP9-439 FP
Clone 5E4
1 mL lyophilized Matrix Metalloproteinase 10
NCL-MMP10 P (HIER)
Clone 9F6
1 mL lyophilized Matrix Metalloproteinase 19
NCL-MMP19 P
The matrix metalloproteinases (MMPs) are a family of zinc-containing
enzymes, which are involved in the degradation of different components of
the extracellular matrix and tissue remodelling. MMPs are expressed widely
during growth and development. The MMPs have been classified into
collagenases, gelatinases and stromelysins, based on the in vitro substrate
specificity. More recently, several MMPs have been identified as
membrane-type specific and matrilysin families. MMPs are multidomain
proteins and are secreted as inactive precursors which are activated by
cleavage of an N-terminal pro-peptide. The major natural inhibitors of
MMPs are tissue inhibitors of matrix metalloproteinases (TIMPs) which
complex with MMPs and are involved in regulating the activity and
activation of individual MMPs. MMP2 (also known as gelatinase A) is able to
initiate degradation of type IV collagen. MMP9 degrades collagen type IV, a
major component of extracellular matrix. MMP9 is also reported to be
expressed in normal kidney tubules, hepatocytes, spermatids, myocytes,
stomach parietal cells, prostatic columnar epithelium and uterine cells.
MMP10 is also known as stromelysin-2 and has a wide range of substrates
including proteoglycan, laminin, fibronectin, collagen IV, collagen IX and the
telopeptides of other collagens. However, some of the more recently
identified MMPs, such as MMP19 - which cleaves aggrecan and cartilage
oligomeric protein, and has several novel structural features, do not fall into
these traditional groupings. MMP19 is reported to be expressed mainly in
placenta, lung, pancreas, ovary, spleen, intestine, breast tissue, smooth
muscle, capillary walls and the endothelial layers of large and medium sized
blood vessels.
Human endometrial adenocarcinoma: immunohistochemical staining for matrix metalloproteinase
2 using NCL-MMP2-507. Note intense staining of malignant epithelial cells and
their secretions. Paraffin section.
MB2 (B Cell Marker)
Clone MB2
1 mL lyophilized NCL-MB2 FP
See also B Cell Marker (MB2) on page 59.
MCAM (CD146)
Clone N1238
1 mL, 0.1 mL lyophilized NCL-CD146 P (HIER) W
See also CD146 (MCAM) on page 87.
Mcl-1
Clone 38G3
1 mL lyophilized NCL-Mcl-1 P
The Mcl-1 gene encodes a protein of approximately 37 kD which shares
significant homology with bcl-2, a protein which blocks programmed cell
death. Mcl-1 protein has been shown to inhibit apoptosis in cells treated
with agents such as UV irradiation or etoposide. Like bcl-2, Mcl-1 protein
can interact with Bax, inhibiting Bax-induced cell death and promoting cell
viability. Although Mcl-1 protein prolongs cell viability, it does not prevent
eventual cell death. Mcl-1 protein is reported to be expressed in epithelial
cells in a variety of tissues including prostate, breast, endometrium,
epidermis, stomach, small intestine, colon and respiratory tract.
Human small intestine: immunohistochemical staining for Mcl-1 protein using NCL-Mcl-1.
Note cytoplasmic staining of differentiated epithelial cells of the villi. Paraffin section.
F Frozen I Immunofluorescence E Electron microscopy
P Paraffin C Flow cytometry O Other applications
W Western blotting
/ 131
Primary Antibodies