AnaSpec Introduces Anti-MMP-1 & Anti-MMP-13 (Hinge) Antibodies

San Jose, CA, July 19, 2007 --( AnaSpec has introduced its newest antibody solutions – anti-MMP-1 (Hinge) and anti-MMP-13 (Hinge) antibodies. 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 customers’ suggestions, AnaSpec’s anti-MMP antibodies are packaged in efficient 50 ul sizes.

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.

Anti-MMP-1 (Hinge), Collagenase-1
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.

For more information, visit

Company Info

AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents (dyes, assay kits, & antibodies), and combinatorial chemistry. Established in 1993, AnaSpec's ISO9001:2000 certified headquarters and manufacturing facilities are located in San Jose, CA.

For more information, visit

1. Woessner, JF. Jr. and CJ. Taplin, J. Biol. Chem. 263, 16918 (1988).
2. Woessner, JF..Jr. FASEB J. 5, 2145 (1991).
3. Goldberg, GI. et al. Ann. NY. Acad. Sci. 580, 375 (1990).
4. Stetler-Stevenson, WG. et al. Annu. Rev. Cell Biol. 9, 541 (1993).
5. Gravallese, EM. et al. Arthritis Rheum. 34, 1076 (1991).
6. Gabison, e. et al. Am. J. Pathology 166, 209 (2005).
7. Freije, JM. et al. J. Biol. Chem. 269, 16766 (1994).

AnaSpec, Inc.
Ping Yang