epitope corresponding to amino acids 426-465 mapping at the C-terminus of MMP-8 of mouse 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-8 (also designated neutrophil collagenase, PMNL collagenase or collagenase-2) degrades fibrillar collagen types I, II and III. Unlike other members of the MMP family, MMP-8 is expressed exclusively in inflammatory conditions. MMP-8 is highly expressed in the postpartum uterus, and it is thought to be involved in the postpartum involution of the uterus. MMP-8 is also the predominant collagenase expressed in ulcers and healing wounds.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of MMP-8 of mouse and rat origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 426-465 mapping at the C-terminus of MMP-8 of mouse origin
Tissue Specificity
epitope corresponding to amino acids 426-465 mapping at the C-terminus of MMP-8 of mouse origin