epitope corresponding to amino acids 178-477 mapping at the C-terminus of MMP-3 of human origin
Modification Notes
The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-3, MMP-10 and MMP-11 (also designated stromelysin-1, -2 and -3 respectively) activate procollagenase. MMP-3 activation of procollagenase can occur via two pathways. Direct activation by MMP-3 is slow and activation by MMP-3 in conjunction with tissue or plasma proteinases is rapid. MMP-10 is expressed in small intestine, and at lower levels in lung and heart. MMP-11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of MMP-3 and MMP-10 of mouse, rat and human origin by WB, IP, IF and ELISA partially cross-reactive with other MMP family members:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 178-477 mapping at the C-terminus of MMP-3 of human origin
Tissue Specificity
epitope corresponding to amino acids 178-477 mapping at the C-terminus of MMP-3 of human origin
Western blot analysis of human recombinant MMP-3 fusion protein.
Application Notes
recommended for detection of MMP-3 and MMP-10 of mouse, rat and human origin by WB, IP, IF and ELISA partially cross-reactive with other MMP family members:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.