MMPs are secreted by diverse connective tissue and pro-inflammatory cells. Typically, these enzymes exhibit minimal expression under normal physiological circumstances. MMPs assume a pivotal role in various cellular processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and immunity. They share a common domain structure, consisting of three key components. First is the pro-peptide, which requires removal to activate the enzyme. Next, there is the catalytic domain, featuring a cysteine switch, where a cysteine residue interacts with zinc, and the haemopexin-like C-terminal domain is linked to the catalytic domain via a flexible hinge region. TIMP-2 (Tissue Inhibitor of Metalloproteinases 2) is indeed a natural inhibitor of the matrix metalloproteinases (MMPs). It forms complexes with certain enzymes within the metalloproteinase family, leading to their irreversible inactivation. TIMP-2 is known to act on a wide range of MMPs, including MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16, and MMP-19. Interestingly, TIMP-2 shares a significant degree of amino acid sequence homology, about 40%, with TIMP-1, especially in their N-terminal domains. This structural similarity underscores their related functions as inhibitors of metalloproteinases, despite some differences in their specific roles and affinities for certain MMPs.
MMPs son secretadas por diversos tejidos conectivos y células proinflamatorias. Normalmente, estas enzimas exhiben una expresión mínima en circunstancias fisiológicas normales. Las MMP asumen un papel fundamental en diversos procesos celulares, incluida la proliferación, migración, diferenciación, angiogénesis, apoptosis e inmunidad celular. Comparten una estructura de dominio común, que consta de tres componentes clave. El primero es el propéptido, que requiere eliminación para activar la enzima. A continuación, está el dominio catalítico, que presenta un interruptor de cisteína, donde un residuo de cisteína interactúa con el zinc, y el dominio C-terminal similar a hemopexina está unido al dominio catalítico a través de una región bisagra flexible. TIMP-2 (inhibidor tisular de metaloproteinasas 2) es de hecho un inhibidor natural de las metaloproteinasas de matriz (MMP). Forma complejos con determinadas enzimas de la familia de las metaloproteinasas, lo que lleva a su inactivación irreversible. Se sabe que TIMP-2 actúa sobre una amplia gama de MMP, incluidas MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14. , MMP-15, MMP-16 y MMP-19. Curiosamente, TIMP-2 comparte un grado significativo de homología de secuencia de aminoácidos, alrededor del 40%, con TIMP-1, especialmente en sus dominios N-terminales. Esta similitud estructural subraya sus funciones relacionadas como inhibidores de metaloproteinasas, a pesar de algunas diferencias en sus funciones específicas y afinidades por ciertas MMP.
Proteins and Peptides
Human
HEK 293 cells
27-220
HEK 293 cells
Lyophilized from a 0.2um filtered solution in PBS with 5% trehalose, pH7.4
Western Blot, ELISA
50μg
200μg
1mg
23.1 kDa
Recombinant
Greater than 95% by SDS-PAGE gel analyses
His tag
Reconstitute with Sterile distilled water
-20°C for 12 months as lyophilized;2-8°C for 1 month under sterile conditions after reconstitution
Timp-2
7 days
CSC 21K, Metalloproteinase inhibitor 2, TIMP 2, TIMP2, TIMP-2
This product is for research use only.
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