| Weight | 1 lbs |
|---|---|
| Dimensions | 9 × 5 × 2 in |
| accession | P22894 |
| express system | HEK293 |
| product tag | C-His |
| purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
| background | Alteration of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) expression has been studied for various cardiac diseases, including dilated cardiomyopathy (DCM), with the significance of surrogate markers of extracellular matrix (ECM) remodeling. MMP-8 was identified only in myocardiocytes, while MMP-9 and TIMP-2 were present in both myocardiocytes and stroma, but with different intensity. The increasing intensity of MMP-8 and TIMP-2 immunoreactions was significantly associated with low HCS. |
| molecular weight | The protein has a predicted MW of 52.2 kDa. Due to glycosylation, the protein migrates to 65-70 kDa based on Tris-Bis PAGE result. |
| available size | 100 µg, 500 µg |
| endotoxin | Less than 1EU per μg by the LAL method. |
Human MMP-8 Protein 3731
$270.00 – $900.00
Summary
- Expression: HEK293
- Active: Yes (catalytic)
- Amino Acid Range: Phe21-Gly467
Human MMP-8 Protein 3731
| protein |
|---|
| Size and concentration 100, 500µg and lyophilized |
| Form Lyophilized |
| Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
| Storage buffer Shipped at ambient temperature. |
| Purity > 95% as determined by Tris-Bis PAGE |
| target relevance |
|---|
| Alteration of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) expression has been studied for various cardiac diseases, including dilated cardiomyopathy (DCM), with the significance of surrogate markers of extracellular matrix (ECM) remodeling. MMP-8 was identified only in myocardiocytes, while MMP-9 and TIMP-2 were present in both myocardiocytes and stroma, but with different intensity. The increasing intensity of MMP-8 and TIMP-2 immunoreactions was significantly associated with low HCS. |
| Protein names Neutrophil collagenase (EC 3.4.24.34) (Matrix metalloproteinase-8) (MMP-8) (PMNL collagenase) (PMNL-CL) |
| Gene names MMP8,MMP8 CLG1 |
| Protein family Peptidase M10A family |
| Mass 9606Da |
| Function Can degrade fibrillar type I, II, and III collagens. |
| Catalytic activity BINDING 91; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /note="in inhibited form"; BINDING 157; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; BINDING 167; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 169; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 174; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 175; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 177; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 179; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 182; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 189; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; BINDING 191; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; BINDING 193; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; BINDING 195; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 197; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 200; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 217; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 221; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 227; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /evidence="ECO:0000269|PubMed:8137810"; BINDING 286; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 378; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000250"; BINDING 425; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000250" |
| Subellular location Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules. |
| Tissues Neutrophils. |
| Domain Th |
| Target Relevance information above includes information from UniProt accession: P22894 |
| The UniProt Consortium |
