Recombinant Human TIMP1 protein (His tag) (Active) is a Human Full Length protein, in the 24 to 207 aa range, expressed in HEK 293, with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors.
CLGI, TIMP, TIMP1, Metalloproteinase inhibitor 1, Erythroid-potentiating activity, Fibroblast collagenase inhibitor, Tissue inhibitor of metalloproteinases 1, EPA, Collagenase inhibitor, TIMP-1
Recombinant Human TIMP1 protein (His tag) (Active) is a Human Full Length protein, in the 24 to 207 aa range, expressed in HEK 293, with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic
=95% by HPLC
Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors.
Belongs to the protease inhibitor I35 (TIMP) family.
The activity of TIMP1 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.
Tissue Inhibitor of Metalloproteinase 1 (TIMP1) is a protein with a molecular mass of approximately 28 kDa. The protein inhibits metalloproteinases by binding to them preventing the breakdown of the extracellular matrix. This action regulates extracellular environment and tissue remodeling. TIMP1 is also known by the name Erythroid-Potentiating Activity (EPA). It is expressed in various tissues including the liver and the brain and can be found in high levels in the blood serum.
TIMP1 plays several essential roles beyond inhibiting metalloproteinases. It supports cell proliferation and influences apoptosis. It is part of a larger TIMP family and does not function as part of a complex per se but interacts closely with matrix metalloproteinases (MMPs). By regulating MMP activity TIMP1 balances processes like tissue growth and inflammatory responses which are important for normal development and repair.
TIMP1 participates in the regulation of the matrix metalloproteinase pathway impacting tissue homeostasis and repair. It closely associates with proteins such as MMP-9 and MMP-2 within this pathway. TIMP1 also plays a role in cytokine signaling pathways which influence immune responses by interacting with other signaling molecules and receptors that govern these pathways.
TIMP1's regulation of MMPs links it to cancer and cardiovascular disease progression. Overexpression of TIMP1 associates with tumor growth and metastasis where it can modulate interactions with other proteins like MMP-9 leading to altered tissue invasion and angiogenesis. Additionally TIMP1 imbalance connects to tissue fibrosis in cardiovascular disorders working in tandem with proteins such as MMP-2 which affects the structural remodeling and function of tissues within the cardiovascular system.
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SDS-PAGE analysis of ab280386.
Fully active determined by its ability to inhibit human MMP2 cleavage of a chromogenic peptide substrate (Mca-PLGL-Dpa-AR-NH2). ED50 is ≤ 3.4 ng/ml, corresponding to specific activity of 2.9 x 10^5 units/mg.
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