MMP11
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
Crystallography grade
MMP11
Spezies: Human
Wirt: Escherichia coli (E. coli)
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
WB, SDS, ELISA, Crys
Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization.
Lagerung
-20 °C,-80 °C
Informationen zur Lagerung
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.
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]
Molekulargewicht
predicted molecular mass of 76.5 kDa after removal of the signal peptide.The apparent molecular mass of MMP11-hFc is 70-100 kDa due to glycosylation.