From one of the world’s largest providers of MMP peptides
come our newest integrated antibody solutions – anti-MMP-1 (Hinge) and anti-MMP-13
(Hinge) antibodies. These antibodies provide a strategic and efficient solution
for your critical MMP research needs.
Strategically raised against the hinge regions of MMP-1
and MMP-13, the epitopes do not overlap the catalytic domain and will not
influence the activity of the MMP ferment in experiments.
In response to our customers’ suggestions, AnaSpec’s anti-MMP
antibodies are packaged in efficient 50 ug sizes.
Designed for Western Blot, ELISA, and IP applications.
Matrix metalloproteinases (MMPs) are a family of highly
homologous protein-degrading zinc dependent enzymes endopeptidases. These enzymes are responsible for the breakdown of connective
tissues and are important in many normal biological processes including embryonic development, angiogenesis,
bone remodeling, menstrual cycle, and wound healing. They are also involved
in pathological processes such as inflammation, cancer, multiple sclerosis, Alzheimer’s,
malignant gliomas, lupus, arthritis, periodontis, emphysema, glomerulonephritis, atherosclerosis,
tissue ulceration, and tissue destruction. Imbalanced secretion of certain MMPs
or disturbances in the differential control of MMP by tissue inhibitor of
MMPs (TIMPs) is implicated in the invasive potential
of malignant tumors.
This family currently includes more than 25 members that can
be divided into collagenases (MMP-1, -8, -13 and -18), gelatinases
(MMP-2 and -9), stromelysins (MMP-3 –7, -10, -11and -13), matrilysins
(MMP-7 and -26), elastins (MMP-12),
and the membrane-type MMPs (MMP-14 to –17, -20, and -21), according
to their structure and substrate specificity.
Rabbit polyclonal anti-MMP-1
(Hinge) antibody was raised against a synthetic
collagenase-1 peptide derived from the hinge region
of human MMP-1. This interstitial collagenase (MMP-1) dissolves extracellular matrix (ECM) and
may initiate and promote angiogenesis. MMP-1 (collagenase 1) is involved in
tumor development and metastasis, and rheumatoid arthritis.
Anti-MMP-1 (Hinge) reacts with MMP-1 at
the molecular weight of 52 kDa as an unglycosylated and
57 kDa as a glycosylated pro-form of MMP-1.
Anti-MMP-13 (Hinge), Collagenase-3
Rabbit anti-MMP-13 (Hinge) polyclonal antibody
was raised against a synthetic collagenase-3 peptide derived from the hinge
region of human MMP-13. MMP-13 (collagenase-3) is a member
of the MMP family of extracellular proteases. Targets of MMP-13 include collagen,
gelatin, aggracan, plasminogen and CXCL12. MMP-13 is secreted as a 60-kDa
proenzyme (as measured by SDS-PAGE), and activated by cleavage to a mature
48-kDa MMP-13. Anti-MMP-13 reacts with MMP-13 at
the molecular weight of approximately 60 kDa at pro-form and 48 kDa at active
form on Western blot.
Related Products
Anti-MMP
antibodies
MMP substrates
SensoLyte™ MMP assay kits
Human
MMP
References:
Woessner, JF. Jr. and
CJ. Taplin, J. Biol. Chem. 263, 16918 (1988).
Woessner, JF..Jr.
FASEB J. 5, 2145 (1991).
Goldberg, GI. et
al. Ann. NY. Acad. Sci. 580, 375 (1990).
Stetler-Stevenson,
WG. et al. Annu. Rev. Cell Biol. 9, 541 (1993).
Gravallese, EM. et al. Arthritis Rheum. 34,
1076 (1991).
Gabison, e. et
al. Am. J. Pathology 166, 209 (2005).
Freije, JM. et al. J. Biol. Chem. 269, 16766
(1994)
