protein

MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi)

HY-P78175

20 μg;50 μg

185;350 USD

MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi)

proteins

HEK293

20 μg;50 μg

185;350 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 (Biotinylated, HEK293, His-Avi) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi) is 688 a.a., with molecular weight of 95-105 kDa.

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.

MMP-9; GELB; CLG4B; MANDP2; Gelatinase B

Greater than 95% as determined by Tris-Bis PAGE.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. Normally 5-8% trehalose is added as protectant before lyophilization.

Room temperature in continental US; may vary elsewhere.