| Target | |
|---|---|
| Synonyms | MMP-11;SL-3;ST3;STMY3 |
| Description | Recombinant human MMP11 protein with C-terminal human Fc tag |
| Delivery | In Stock |
| Uniprot ID | P24347 |
| Expression Host | HEK293 |
| Tag | C-Human Fc Tag |
| Molecular Characterization | MMP11(Arg32-Leu488) hFc(Glu99-Ala330) |
| Molecular Weight | The protein has a predicted molecular mass of 76.5 kDa after removal of the signal peptide.The apparent molecular mass of MMP11-hFc is approximately 70-100 kDa due to glycosylation. |
| Purity | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
| Formulation & Reconstitution | Lyophilized from sterile PBS, pH 7.4. Normally 5 % – 8% trehalose is added as protectants before lyophilization. Please see Certificate of Analysis for specific instructions of reconstitution. |
| Storage & Shipping | 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. |
| Background | 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. [provided by RefSeq, Jul 2008] |
| Usage | Research use only |
| Conjugate | Unconjugated |
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