Monkey Metalloproteinase Inhibitor 3 (TIMP3) ELISA Kit is an ELISA Kit for the in vitro quantitative measurement of Monkey Metalloproteinase Inhibitor 3 (TIMP3) concentrations in serum, plasma, tissue homogenates, cell lysates, cell culture supernatants and other biological fluids. This assay has high sensitivity and excellent specificity for detection of Tissue Inhibitors Of Metalloproteinase 3 (TIMP3)No significant cross-reactivity or interference between Tissue Inhibitors Of Metalloproteinase 3 (TIMP3) and analogues was observed.
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
ELISA Kits
Metalloproteinase Inhibitor 3 (TIMP3)
Monkey
0.312 ng/ml - 20 ng/ml
< 0.12 ng/ml
Sandwich
Quantitative
Colorimetric
Serum,Plasma,Tissue homogenates,Cell lysates,Other biological fluids
96 tests
5 × 96 tests
10 × 96 tests
Enviado a 4 °C. Una vez recibido, almacene el kit de acuerdo con las instrucciones citadas en el manual del kit
TIMP3
No
This product is for research use only. <p></p> The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. <p></p> Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein.
Precio a consultar
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