Recombinant human TIMP2 protein is a Human Full Length protein, in the 2 to 220 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on 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.
Metalloproteinase inhibitor 2, CSC-21K, Tissue inhibitor of metalloproteinases 2, TIMP-2, TIMP2
Recombinant human TIMP2 protein is a Human Full Length protein, in the 2 to 220 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
Purity is greater than 95% by SDS-PAGE gel and HPLC analyses.Endotoxin level is less than 0.1 ng per µg (1EU/µg).
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on 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.
Belongs to the protease inhibitor I35 (TIMP) family.
The activity of TIMP2 is dependent on the presence of disulfide bonds.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex (can be stored at 4C for up to 1 week).
For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20C to -80C.
TIMP2 also known as Tissue Inhibitor of Metalloproteinases 2 mechanistically inhibits the activity of matrix metalloproteinases (MMPs). It binds to MMPs regulating the extracellular matrix's remodeling. The protein has a molecular mass of around 21 kDa. TIMP2 is expressed in various tissues including the brain liver and kidneys where it maintains a balance between matrix degradation and production.
TIMP2 plays a significant role in tissue maintenance and repair by controlling extracellular matrix turnover. It forms complexes with MMPs such as MMP-2 inhibiting their proteolytic activities. The protein is also involved in cell proliferation and differentiation affecting processes like angiogenesis and wound healing. Its regulatory function aids in maintaining tissue homeostasis and preventing excessive matrix breakdown.
TIMP2 is integral to the matrix metalloproteinase pathway and the regulation of endothelial cell migration. The protein interacts closely with other MMPs influencing their activation and modulation. Through these pathways TIMP2 holds an important position in cellular migration and signaling ensuring precise matrix remodeling in response to physiological needs.
TIMP2 has significant links with cancer and fibrosis. Dysregulation of TIMP2 expression or its imbalance with MMPs can contribute to tumor progression and metastasis due to uncontrolled matrix degradation. Additionally abnormal TIMP2 levels associate with fibrotic diseases where excessive tissue deposition occurs. TIMP2's interaction with proteins like MMP-9 and MMP-2 highlights its involvement in these pathological conditions.
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