|Tested species reactivity||Human|
|Published species reactivity||Bovine|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Synthetic peptide derived from the C-terminus of the human MMP1.|
|Contains||0.08% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1-5 µg/ml|
|Western Blot (WB)||1-2 µg/ml|
|Western Blot (WB)||See 1 publications below|
A suggested positive control for this product is colon, esophageal or gastric tissues.
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-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
Effect of stages of lactation on the concentration of a 90-kilodalton heat shock protein in bovine mammary tissue.
MA1-12891 was used in western blot to investigate the differences of HSP90 expression in cow mammary tissue at various lactation stages
|Watanabe A,Miyamoto T,Katoh N,Takahashi Y||Journal of dairy science (80:2372)||1997|