protein

MMP-9 Protein, Human (P. pastoris, His)

HY-P700572

20 μg;50 μg;100 μg

160;300;480 USD

MMP-9 Protein, Human (P. pastoris, His)

proteins

P. pastoris

20 μg;50 μg;100 μg

160;300;480 USD

MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (P. pastoris, His) is the recombinant human-derived MMP-9 protein, expressed by P. pastoris , with N-6*His labeled tag.

Human

MMP-9 protein, a matrix metalloproteinase, plays a crucial role in the localized breakdown of the extracellular matrix and facilitates leukocyte migration. It has been suggested that MMP-9 may also be involved in bone osteoclastic resorption. Additionally, MMP-9 cleaves KiSS1 at a Gly- -Leu bond and NINJ1 to generate the secreted form of ninjurin-1. Furthermore, it is known to cleave type IV and type V collagen, resulting in the production of large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. While MMP-9 degrades fibronectin, it does not have an impact on laminin or Pz-peptide.

rHuMatrix metalloproteinase-9/MMP-9, His; Matrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; MMP9

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 0.5 M NaCl, 6%Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.