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103000
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
105000
-
the molecular mass of recombinant MMP-9 is approximately 105000 Da, SDS-PAGE
135000
-
neutrophil gelatinase-associated lipocalin-MMP-9 complex, SDS-PAGE
150000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 150000 Da band represents a complex of MMP-9 with itself, other matrix metallproteinases, or other molecules such as TIMPs or inflammatory molecules
200000
-
the molecular weight of proMMP-9 is about 200000 Da, SDS-PAGE
20947
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
210000
dimeric form, SDS-PAGE
228300
enzyme multimer/trimer, PAGE, structure analysis by AFM
230000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
65000 - 82000
major circulating MMP-9 enzyme forms: 92 kDa proMMP-9, and active 82 kDa and 65 kDa enzyme forms
66000
-
active form of MMP-9, SDS-PAGE
67000
-
active form of MMP-9, SDS-PAGE
70795
-
x * 70795, calculated, enzyme mutant E402A, x * 20947, calculated, isolated enzyme collagen-binding domain
72000
-
active form of MMP-9, SDS-PAGE
78000
-
active form of MMP-9, SDS-PAGE
80000
-
x * 80000, deglycosylated enzyme, SDS-PAGE, x * 230000, glycosylated enzyme, SDS-PAGE
85000
-
85000 Da polypeptide in both cellular and secreted parasite extracts, activated form of MMP-9, SDS-PAGE
87000
-
active form of MMP-9
89300
x * 89300, about, SDS-PAGE, the natural zymogen proMMP-9 occurs as monomers, homomultimers and heterocomplexes. MMP-9 homomultimers are reduction-sensitive trimers, three-dimensional structure molecular modeling, overview. Homomultimerization of the enzyme involves cysteine bridge formation. The zymogen proMMP-9 monomer includes the propeptide, the fibronectin-like domain, the Zn2+ -binding domain, the catalytic domain, the flexible OG domain, and the haemopexin-like domain
95000
-
proMMP-9, SDS-PAGE
96000
-
proMMP-9, SDS-PAGE
130000
-
-
130000
-
x * 92000,enzyme form 1, SDS-PAGE, x * 130000, enzyme form 2, SDS-PAGE, x * 225000, enzyme form 3, SDS-PAGE
225000
-
-
225000
-
x * 92000,enzyme form 1, SDS-PAGE, x * 130000, enzyme form 2, SDS-PAGE, x * 225000, enzyme form 3, SDS-PAGE
65000
-
4-aminophenylmercuric acetate produces not only the 82000 Da active enzyme but also a C-terminal truncated form of approximately 65000 Da with activity comparable to that of the 82000 Da form
65000
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE
82000
-
active enzyme, gelatin zymography
82000
-
activated form of MMP-9, SDS-PAGE
82000
-
x * 92000, full-length pro-MMP-9, SDS-PAGE, x * 82000, processed active MMP-9, SDS-PAGE
82000
-
2 * 82000, active MMP-9, SDS-PAGE
82000
-
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE
82000
x * 65000, active matured, truncated enzyme form lacking both the N- and C-terminal domains, SDS-PAGE, x * 82000, activated mature enzyme, SDS-PAGE
84000
-
MMP-9 active enzyme, SDS-PAGE
84000
-
1 * 92000, human SC40-transformed lung cells, proenzyme, SDS-PAGE, 1 * 84000, human SC40-transformed lung cells, activated form, SDS-PAGE
84000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 84000, activated MMP-9, SDS-PAGE
86000
-
x * 103000, about, pro-MMP9, SDS-PAGE, x * 86000, about, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
86000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
88000
-
active form of MMP-9, SDS-PAGE
92000
-
-
92000
-
human SC40-transformed lung cells, gel filtration, glycosylated proenzyme can be activated by organomercurials by removal of 73 amino acids
92000
monomeric form, SDS-PAGE
92000
-
gelatinolytic activity of MMP-9 is observed at two molecular weights, 150000 Da and 92000 Da, the 92000 Da form corresponds to the MMP-9 pro form
92000
-
MMP-9 proenzyme, SDS-PAGE
92000
-
proenzyme, gelatin zymography
92000
-
activated MMP-9, SDS-PAGE
92000
-
inactive enzyme form
92000
-
inactive form of MMP-9, SDS-PAGE
92000
-
inactive pro-MMP-9, SDS-PAGE
92000
-
pro-form of MMP-9, SDS-PAGE
92000
-
pro-MMP-9, SDS-PAGE
92000
-
2 * 92000, pro-MMP-9, SDS-PAGE
92000
-
x * 92000, full-length pro-MMP-9, SDS-PAGE, x * 82000, processed active MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 84000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP-9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
x * 92000, pro-MMP9, SDS-PAGE, x * 86000, activated MMP-9, SDS-PAGE
92000
-
2 * 92000, proMMP-9, SDS-PAGE
92000
-
1 * 92000, pro-enzyme, SDS-PAGE, 1 * 82000, recombinant truncated mutant MMP-9, SDS-PAGE
94000
-
-
94000
-
pro-MMP9, SDS-PAGE
97000
-
SDS-PAGE
97000
-
active enzyme form, gelatin gel zymography
97000
-
active form of MMP-9, SDS-PAGE
97000
-
97000 Da protein band in cellular extract, SDS-PAGE