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Proteolysis & Protein Degradation
| Alternative Name | 1-(5-Chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine . HCl |
|---|---|
| CAS | 105637-50-1 |
| Couple Type | Inhibitor |
| Purity | ≥98% (TLC) |
| Application | Activity assay, Colorimetric detection, HTS |
|---|
| Application | Activity assay, Fluorescent detection, HTS |
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| Purity | ≥97% (HPLC) |
|---|
| Alternative Name | Matrix metalloproteinase 1, Interstitial collagenase, Fibroblast collagenase |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-1 (MMP-1, interstitial collagenase, fibroblast collagenase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-1 (Phe100-Gln268) with a C-terminal purification tag. |
| Alternative Name | Matrix metalloproteinase 1, Interstitial collagenase, Fibroblast collagenase |
|---|---|
| Purity | ≥90% (SDS-PAGE, Western blot) |
| Source | Isolated from human rheumatoid synovial fibroblasts. Requires activation. |
| Alternative Name | Matrix metalloproteinase 10, Stromelysin-2 |
|---|---|
| Source | Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag. This comprises an active form of MMP-10 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 11, Stromelysin-3 |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-11 (MMP-11, Stromelysin-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-11 (Phe98-Ser266, NM_005940) with a C-terminal purification tag. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. It may be an important link between obesity and cancer. |
| Alternative Name | Matrix metalloproteinase 12, Metalloelastase, Macrophage elastase |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase; often confused with neutrophil elastase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-12 (Phe99-Leu271, NM_002426) with a C-terminal purification tag. |
| Alternative Name | Matrix metalloproteinase 12, Metalloelastase, Macrophage elastase |
|---|---|
| Application | WB |
| Host | Rabbit |
| Species Reactivity | Human, Mouse, Rat |
| Alternative Name | Matrix metalloproteinase 13, Collagenase-3 |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-13 (MMP-13, collagenase-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-13 (Tyr104-Asn274, NM_002427) with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-13 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 | 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) |