Rabbit Polyclonal against the TIMP3 protein.
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-3 (Tissue Inhibitor of Metalloproteinases 3) serves as a natural inhibitor of matrix metalloproteinases (MMPs). It has the ability to form complexes with various metalloproteinases, including collagenases, and inactivates them irreversibly by binding to their catalytic zinc cofactor. This binding effectively halts the enzymatic activity of these MMPs. TIMP-3 is known to act on several MMPs, including MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14, and MMP-15. Its role in forming tissue-specific acute responses to remodeling stimuli underscores its importance in regulating extracellular matrix dynamics and tissue maintenance.
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-3 (inhibidor tisular de metaloproteinasas 3) sirve como inhibidor natural de las metaloproteinasas de matriz (MMP). Tiene la capacidad de formar complejos con varias metaloproteinasas, incluidas las colagenasas, y las inactiva irreversiblemente uniéndose a su cofactor catalítico de zinc. Esta unión detiene efectivamente la actividad enzimática de estas MMP. Se sabe que TIMP-3 actúa sobre varias MMP, incluidas MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 y MMP-15. Su papel en la formación de respuestas agudas específicas de tejido a estímulos de remodelación subraya su importancia en la regulación de la dinámica de la matriz extracelular y el mantenimiento del tejido
Primary Antibodies
Polyclonal
Human
Metalloproteinase Inhibitor 3 (TIMP3)
Rabbit
Unconjugated
Lyophilized
ELISA, WB, IHC
Purified by antigen affinity column chromatography.
Prior to lyophilization: 1% BSA and 0.02% NaN3.
100 µg
Store at -20 °C. Avoid repeated freeze/thaw cycles.
TIMP3
No
Shipped within 7-15 working days.
NM_000362
This product is for research use only.
Polyclonal Antibody to Tissue Inhibitors of Metalloproteinase 3 (TIMP3).
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