Released on = July 17, 2007, 10:21 am

Press Release Author = AnaSpec Inc.

Industry = Biotech

Press Release Summary = 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.

Press Release Body = July 13, 2007 - San Jose, CA
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 http://www.anaspec.com/products/promotions.asp?col

Web Site = http://www.anaspec.com

Contact Details = AnaSpec Inc.
Ping Yang
ping@anaspec.com
1-408-452-5055