Anti-MMP-7 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC-P, E |
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Primary Accession | P09237 |
Host | Rabbit |
Reactivity | Human |
Clonality | Polyclonal |
Format | Lyophilized |
Description | Rabbit IgG polyclonal antibody for Matrilysin(MMP7) detection. Tested with WB, IHC-P, ELISA in Human. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 4316 |
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Other Names | Matrilysin, 3.4.24.23, Matrin, Matrix metalloproteinase-7, MMP-7, Pump-1 protease, Uterine metalloproteinase, MMP7, MPSL1, PUMP1 |
Calculated MW | 29677 MW KDa |
Application Details | ELISA , 0.1-0.5 µg/ml, Human, - Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat Western blot, 0.1-0.5 µg/ml, Human |
Subcellular Localization | Secreted, extracellular space, extracellular matrix . |
Protein Name | Matrilysin |
Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
Immunogen | E.coli-derived human MMP7 recombinant protein (Position: M1-K267). Human MMP7 shares 71% amino acid (aa) sequence identity with both mouse and rat MMP7. |
Purification | Immunogen affinity purified. |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Sequence Similarities | Belongs to the peptidase M10A family. |
Name | MMP7 |
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Synonyms | MPSL1, PUMP1 |
Function | Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. |
Cellular Location | Secreted, extracellular space, extracellular matrix |

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Provided below are standard protocols that you may find useful for product applications.
Background
Matrix metalloproteinase-7 (MMP-7) previously called putative metalloproteinase I (PUMP1) or matrilysin. The MMP-7 gene has been identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. The MMP-7 protein has 267 amino acids and is significantly shorter than stromelysin or collagenase (477 and 469 amino acids, respectively). Matrix metalloproteinases play a crucial role in tumor invasion and metastasis. MMP-7, a member of the matrix metalloproteinase family, is structurally different from the other matrix metalloproteinases by virtue of the absence of a conserved COOH-terminal protein domain. In addition, MMP-7 mRNA is regulated in a specific and distinct manner in normal and malignant tissues. MMP-7 has been shown to correlate with nodal or distant metastasis in colorectal carcinomas, however, its implication in early invasive colorectal carcinomas has not been determined. MMP-7 is also a mediator of pulmonary fibrosis and a potential therapeutic target. The standard product used in this kit is recombinant human MMP-7, consisting of 250 amino acids with the molecular mass of 28KDa. The detected MMP-7 includes zymogen and active enzyme.

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