protein

MMP-26 Protein, Human

HY-P76498

20 μg;100 μg

304;850 USD

MMP-26 Protein, Human

proteins

E. coli

20 μg;100 μg

304;850 USD

The MMP-26 protein has broad substrate specificity and hydrolyzes type IV collagen, fibronectin, fibrinogen, β-casein, type I gelatin, and α-1 protease inhibitors. The versatility of this enzyme suggests involvement in the degradation and remodeling of various extracellular matrix components. MMP-26 Protein, Human is the recombinant human-derived MMP-26 protein, expressed by E. coli , with tag free. The total length of MMP-26 Protein, Human is 172 a.a., with molecular weight of ~19 KDa.

Human

The MMP-26 protein demonstrates a broad substrate specificity, as it may hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin, and alpha-1 proteinase inhibitor. Its capacity to enzymatically cleave these diverse substrates indicates its potential involvement in the degradation and remodeling of various extracellular matrix components. Additionally, MMP-26 is capable of activating progelatinase B, suggesting a regulatory role in modulating the activity of other matrix metalloproteinases. The diverse substrate hydrolysis and activation capabilities of MMP-26 underscore its significance in the dynamic processes of tissue remodeling and homeostasis within the extracellular matrix.

Matrix metalloproteinase-26; MMP-26; Endometase; Matrilysin-2

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 2 mM CaCl 2 , pH 7.8. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.