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Cellular Analysis
| Alternative Name | Collagenase-3, Matrix metalloproteinase 13 |
|---|---|
| Application | ELISA, WB |
| Host | Rabbit |
| Species Reactivity | Human |
| Alternative Name | Matrix metalloproteinase 13, Collagenase-3 |
|---|---|
| Source | Produced in insect cells. Primarily full length latent MMP-13, with some active forms present. Produced in a baculovirus expression system. |
| Alternative Name | PB4, N4,N6-Bis(4-fluoro-3-methylbenzyl)pyrimidine-4,6-dicarboxamide, Pyrimidine-4,6-dicarboxylic acid, bis-(4-fluoro-3-methyl-benzylamide), 4-N,6-N-bis[(4-fluoro-3-methylphenyl)methyl]pyrimidine-4,6-dicarboxamide |
|---|---|
| CAS | 544678-85-5 |
| Couple Type | Inhibitor |
| Purity | ≥99% (HPLC) |
| Alternative Name | Matrix metalloproteinase 14, Membrane type matrix metalloproteinase 1, MT-1 MMP |
|---|---|
| Source | Produced in E.coli. Active Matrix Metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase 1, MT1-MMP) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-14 (Tyr112-Arg298, NM_004995) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-14 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. |
| Alternative Name | Matrix metalloproteinase 19, RASI |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E.coli. Active recombinant MMP-19. |
| Alternative Name | Matrix metalloproteinase 2, Gelatinase A, 72 kDa Type IV collagenase |
|---|---|
| Purity | ≥90% (SDS-PAGE) |
| Source | Produced in yeast. Active recombinant matrix metalloproteinase-2 (MMP-2, gelatinase A, 72kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Tyr110-Asp452, which comprises the catalytic/fibronectin domain of human MMP-2, with a C-terminal purification tag. |
| Alternative Name | Matrix metalloproteinase 2, Gelatinase A, 72 kDa Type IV collagenase |
|---|---|
| Source | Isolated from mouse fibroblasts. Primarily latent form. |
| Alternative Name | Matrix metalloproteinase 2, Gelatinase A, 72 kDa Type IV collagenase |
|---|---|
| Purity | ≥90% (SDS-PAGE, Western blot) |
| Source | Isolated from human rheumatoid synovial fibroblasts. Requires activation. |
| Alternative Name | Matrix metalloproteinase 20, Enamelysin |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active recombinant matrix metalloproteinase-20 (MMP-20, enamelysin) cloned from human cDNA. The enzyme consists of residues Tyr108-Phe276 (NM_004771), which comprises the catalytic domain of human MMP-20, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-20 which lacks the C-terminal hemopexin domain. |
| Alternative Name | Matrix metalloproteinase 3, Stromelysin-1, Transin-1 |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-3 (MMP-3, stromelysin-1, transin) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-3 (Phe100-Thr272, NM_002422) with a C-terminal purification tag. |
| Alternative Name | Matrix metalloproteinase 7, Matrilysin, Pump |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-7 (MMP-7, matrilysin, pump) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-7 (Tyr95-Lys267, NM_002423) with a C-terminal purification tag. |
| Alternative Name | Matrix metalloproteinase 8, Neutrophil collagenase, Collagenase-2 |
|---|---|
| Purity | ≥90% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-8 (MMP-8, neutrophil collagenase, collagenase-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-8 (Phe99-Gln269, NM_002424) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-8 which lacks the C-terminal hemopexin domain1. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. |
| Alternative Name | Matrix metalloproteinase 9, Gelatinase B, 92 kDa Type IV collagenase |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active recombinant matrix metalloproteinase-9 (MMP-9, gelatinase B, 92 kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Phe107-Pro449 (NM_004994), which comprises the catalytic/fibronectin domain of human MMP-9, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-9 which lacks the C-terminal hemopexin domain. Activity toward its targets, such as gelatin, casein, or peptide substrates, is unaffected. |
Metabolism
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Neuroscience
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Live Cell Analysis
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Apoptosis
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Immunology
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Autophagy
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