Recombinant human MMP11 protein with C-terminal human Fc tag
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| Amount : | 50 µg |
| Purification : | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
| Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization. |
| Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
| Alternative Name : | SL-3; ST3; STMY3 |
Expression Host : HEK293
The protein has a predicted molecular mass of 68.5 kDa after removal of the signal peptide.
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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.
The protein has a predicted molecular mass of 68.5 kDa after removal of the signal peptide.
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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.
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