Overview |
bs-0423r-100ul |
MMP-7 Polyclonal Antibody |
WB, ELISA, FCM, IHC-P, IHC-F, IF(IHC-P), IF(IHC-F), IF(ICC) |
Human, Mouse |
Rat |
Specifications |
Unconjugated |
Rabbit |
KLH conjugated synthetic peptide derived from mouse MMP7 |
151-250/269 |
Polyclonal |
IgG |
1ug/ul |
Purified by Protein A. |
0.01M TBS(pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
Target |
Secreted, Extracellular matrix |
Matrilysin; Matrilysin uterine; Matrin; Matrix Metalloproteinase 7; MMP 7; MMP7; MPSL1; PUMP 1; Pump 1 protease; PUMP1; Uterine Matrilysin; Uterine metalloproteinase. |
Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas. |
Application Dilution |
WB |
1:300-5000 |
ELISA |
1:500-1000 |
FCM |
1:20-100 |
IHC-P |
1:200-400 |
IHC-F |
1:100-500 |
IF(IHC-P) |
1:50-200 |
IF(IHC-F) |
1:50-200 |
IF(ICC) |
1:50-200 |