MMP2 Mouse
72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Greater than 85.0% as determined by SDS-PAGE.
Description
MMP2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 644 amino acids (30-662 aa) and having a molecular mass of 72.4kDa.
MMP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
MMP-2, also known as gelatinase A, is secreted by various cell types, including fibroblasts, cardiomyocytes, and myofibroblasts. It exhibits a broad substrate specificity, acting on molecules such as elastin, collagen, fibroblast growth factor, endothelin, MMP-9, plasminogen, MMP-13, and TGF-beta. This wide range of substrates suggests that MMP-2 plays diverse roles in biological processes. Following myocardial infarction (MI), MMP-2 activity increases by day four and reaches its peak by day seven.
MMP2 Mouse, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 644 amino acids (residues 30-662). It has a molecular weight of 72.4 kDa. The protein features a 6-amino acid Histidine tag fused to its C-terminus. Purification is achieved using proprietary chromatographic techniques.
The provided MMP2 solution has a concentration of 0.25 mg/ml. It is formulated in a buffer consisting of 10% glycerol and Phosphate-Buffered Saline (PBS) at a pH of 7.4.
For short-term storage (2-4 weeks), the MMP2 solution should be kept refrigerated at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein, such as 0.1% HSA (human serum albumin) or BSA (bovine serum albumin), is advised. Repeated freezing and thawing of the solution should be avoided.
The purity of the MMP2 Mouse protein is determined to be greater than 85.0% using SDS-PAGE analysis.
72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
ADPEFAPSPI IKFPGDVAPK TDKELAVQYL NTFYGCPKES CNLFVLKDTL KKMQKFFGLP QTGDLDQNTI ETMRKPRCGN PDVANYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARALKVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGREY SSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NADGQPCKFP FRFQGTSYNS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRNDGKVW CATTTNYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS HDDIKGIQEL YGPSPDADTD TGTGPTPTLG PVTPEICKQD IVFDGIAQIR GEIFFFKDRF IWRTVTPRDK PTGPLLVATF WPELPEKIDA VYEAPQEEKA VFFAGNEYWV YSASTLERGY PKPLTSLGLP PDVQQVDAAF NWSKNKKTYI FAGDKFWRYN EVKKKMDPGF PKLIADSWNA IPDNLDAVVD LQGGGHSYFF KGAYYLKLEN QSLKSVKFGS IKSDWLGCHH HHHH
Product Science Overview
Matrix Metalloproteinase-2 (MMP-2), also known as gelatinase A or type IV collagenase, is a member of the matrix metalloproteinase (MMP) family of enzymes. These enzymes are involved in the degradation of the extracellular matrix (ECM) and play crucial roles in various physiological and pathological processes.
MMP-2 is a 72 kDa protein that contains several distinct domains:
- Signal Peptide Domain: Targets the enzyme for secretion.
- Pro-peptide Domain: Removed upon activation of the enzyme.
- Catalytic Domain: Contains the gelatin-binding domain essential for its enzymatic activity .
MMP-2 cleaves a variety of substrates, including gelatin, type IV, V, VII, X, and XI collagens, fibronectin, elastin, laminin, and proteoglycans . It also cleaves native type I collagen into specific fragments .
MMP-2 plays essential roles in:
