Recombinant Human MMP9(20-707) Protein, His Tag
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| Amount : | 50 µg |
| Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8% trehalose is added as protectants before lyophilization. |
| Storage condition : | Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature. |
| Uniprot ID : | P14780 |
| Alternative Name : | CLG4B, GELB, MANDP2, MMP-9 |
Molecular Characterization: MMP9(20-707)?Ala20-Asp707?+6×His tag
Molecular Weight: The protein has a predicted molecular mass of 77.2 kDa after removal of the signal peptide. The apparent molecular mass of MMP9(20-707)-His is approximately 70-100 kDa due to glycosylation.
Description: Recombinant human MMP9(20-707) protein with C-terminal 6×His tag
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]
Molecular Weight: The protein has a predicted molecular mass of 77.2 kDa after removal of the signal peptide. The apparent molecular mass of MMP9(20-707)-His is approximately 70-100 kDa due to glycosylation.
Description: Recombinant human MMP9(20-707) protein with C-terminal 6×His tag
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]
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