protein

TIMP-2 Protein, Human (HEK293)

HY-P73442

20 μg

300 USD

TIMP-2 Protein, Human (HEK293)

proteins

HEK293

20 μg

300 USD

TIMP-2 protein is a tissue inhibitor of metalloproteinases that can bind and inactivate various metalloproteinases, including collagenases, such as 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. It interacts with MMP2 through its C-terminal region, specifically targets the C-terminal PEX domain and inhibits MMP2 activity. TIMP-2 Protein, Human (HEK293) is the recombinant human-derived TIMP-2 protein, expressed by HEK293 , with tag free. The total length of TIMP-2 Protein, Human (HEK293) is 194 a.a., with molecular weight of ~20 kDa.

Human

TIMP-2, a tissue inhibitor of metalloproteinases, forms stable complexes with various metalloproteinases, particularly collagenases, and exerts irreversible inactivation by binding to their catalytic zinc cofactor. This regulatory action encompasses a spectrum of metalloproteinases, 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. Notably, TIMP-2's intricate interactions extend to MMP2, where binding occurs via the C-terminal region, specifically interacting with the C-terminal PEX domain of MMP2, resulting in the inhibition of MMP2 activity. This dynamic interplay underscores TIMP-2's role as a versatile modulator in regulating the activity of metalloproteinases critical for extracellular matrix remodeling and tissue homeostasis.

TIMP-2; Metalloproteinase inhibitor 2; CSC-21K; TIMP2

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.