protein

MMP-8 Protein, Human (HEK293)

HY-P73298

20 μg;100 μg

429;1200 USD

MMP-8 Protein, Human (HEK293)

proteins

HEK293

20 μg;100 μg

429;1200 USD

MMP-8, also known as matrix metalloproteinase-8 or collagenase-2, is recognized for its enzymatic abilities, particularly its ability to break down fibrillar types I, II, and III collagen. This enzymatic activity suggests that MMP-8 plays an important role in the remodeling and turnover of collagen-rich tissues such as connective tissue, cartilage, and bone. MMP-8 Protein, Human (HEK293) is the recombinant human-derived MMP-8 protein, expressed by HEK293 , with N-Met labeled tag. The total length of MMP-8 Protein, Human (HEK293) is 447 a.a., with molecular weight of ~65 kDa.

Human

MMP-8, also referred to as matrix metalloproteinase-8 or collagenase-2, is recognized for its enzymatic capabilities and specifically its ability to break down fibrillar type I, II, and III collagens. This enzymatic activity suggests that MMP-8 plays a significant role in the remodeling and turnover of collagen-rich tissues, such as connective tissues, cartilage, and bone. By degrading these fibrillar collagens, MMP-8 can contribute to processes such as tissue remodeling, wound healing, and inflammation resolution. Understanding the precise functions and regulation of MMP-8 can provide valuable insights into its involvement in collagen metabolism and tissue remodeling, potentially offering therapeutic opportunities for conditions characterized by abnormal collagen degradation or accumulation.

Neutrophil collagenase; MMP-8; PMNL-CL; CLG1

Greater than 90% 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.