epitope corresponding to amino acids 1-267 representing full length MMP-7 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-7 (also designated Pump-1, matrilysin or uterine metalloproteinase) degrades casein, fibronectin and gelatin types I, III, IV and V. MMP-7 mRNA is produced exclusively by epithelial cells in mouse and expression is restricted to specific organs, suggesting that in addition to matrix degradation and remodeling, MMP-7 may be involved in the differentiated function of these organs.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of MMP-7 of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA may cross-react with other MMP family members:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-267 representing full length MMP-7 of human origin
Tissue Specificity
epitope corresponding to amino acids 1-267 representing full length MMP-7 of human origin
recommended for detection of MMP-7 of human and, to a lesser extent, mouse and rat origin by WB, IP, IF and ELISA may cross-react 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.