Mouse MMP-8 Protein (pro form) 3608

Additional Information:
inaccessionO70138|express systemHEK293|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundAlteration 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 weightThe protein has a predicted MW of 51.9 kDa. Due to glycosylation, the protein migrates to 65-70 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Mouse MMP-8 Protein (pro form) 3608proteinSize and concentration100, 500g and liquidFormLiquidStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped with dry ice.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceAlteration 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 namesNeutrophil collagenase (EC 3.4.24.34) (Collagenase 2) (Matrix metalloproteinase-8) (MMP-8)Gene namesMmp8,Mmp8Protein familyPeptidase M10A familyMass10090DaFunctionCan degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.Catalytic activityBINDING 91; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”2″; /ligand_note=”catalytic”; /note=”in inhibited form”; /evidence=”ECO:0000250″; BINDING 157; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 167; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 169; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 174; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250″; BINDING 175; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250″; BINDING 177; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250″; BINDING 179; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250″; BINDING 182; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 189; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 191; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 193; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 195; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”1″; /evidence=”ECO:0000250″; BINDING 197; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250″; BINDING 200; /ligand=”Ca(2+)”; /ligand_id=”ChEBI:CHEBI:29108″; /ligand_label=”2″; /evidence=”ECO:0000250″; BINDING 217; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”2″; /ligand_note=”catalytic”; /evidence=”ECO:0000250″; BINDING 221; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”2″; /ligand_note=”catalytic”; /evidence=”ECO:0000250″; BINDING 227; /ligand=”Zn(2+)”; /ligand_id=”ChEBI:CHEBI:29105″; /ligand_label=”2″; /ligand_note=”catalytic”; /evidence=”ECO:0000250″; 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 locationCytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules and released during inflammatory conditions.TissuesNeutrophils. Expressed in uterus. Low levels in kidney and muscle.DomainThTarget Relevance information above includes information from UniProt accession: O70138The UniProt Consortium|