MMP9 Mouse
Sf9, Baculovirus cells.
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Greater than 85% as determined by SDS-PAGE.
Description
MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a.) and having a molecular mass of 79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Matrix metalloproteinase 9 (MMP9) is a member of the matrix metalloproteinase family. MMPs play a crucial role in the breakdown of the extracellular matrix, contributing to various physiological processes such as wound healing, bone development, and reproduction. However, MMP9 is also implicated in pathological conditions, including metastasis, arthritis, and intracerebral hemorrhage.
Recombinant mouse MMP9, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain. It comprises 717 amino acids (20-730 a.a.) and has a molecular weight of 79.3 kDa. The protein is engineered with a 6-amino acid Histidine tag at the C-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
The MMP9 Mouse protein solution is provided at a concentration of 0.25 mg/ml and contains the following components: 20 mM Tris-HCl (pH 7.5), 10 mM CaCl2, 100 mM NaCl, 0.05% Brij35, and 10% glycerol.
The purity of the MMP9 Mouse protein is determined to be greater than 85% as assessed by SDS-PAGE analysis.
The biological activity of MMP9 is defined as its ability to cleave a specific substrate, Mca-PLGLDpa-AR-NH2. One unit of activity is defined as the amount of enzyme required to cleave 1 pmol of this substrate per minute at a pH of 7.5 and a temperature of 25°C. The specific activity of MMP9 Mouse is greater than 500 pmol/min/µg. |
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Sf9, Baculovirus cells.
APYQRQPTFV VFPKDLKTSN LTDTQLAEAY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS QTLKAIRTPR CGVPDVGRFQ TFKGLKWDHH NITYWIQNYS EDLPRDMIDD AFARAFAVWG EVAPLTFTRV YGPEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGAGVQ GDAHFDDDEL WSLGKGVVIP TYYGNSNGAP CHFPFTFEGR SYSACTTDGR NDGTPWCSTT ADYDKDGKFG FCPSERLYTE HGNGEGKPCV FPFIFEGRSY SACTTKGRSD GYRWCATTAN YDQDKLYGFC PTRVDATVVG GNSAGELCVF PFVFLGKQYS SCTSDGRRDG RLWCATTSNF DTDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPLYSYLEGF PLNKDDIDGI QYLYGRGSKP DPRPPATTTT EPQPTAPPTM CPTIPPTAYP TVGPTVGPTG APSPGPTSSP SPGPTGAPSP GPTAPPTAGS SEASTESLSP ADNPCNVDVF DAIAEIQGAL HFFKDGWYWK FLNHRGSPLQ GPFLTARTWP ALPATLDSAF EDPQTKRVFF FSGRQMWVYT GKTVLGPRSL DKLGLGPEVT HVSGLLPRRL GKALLFSKGR VWRFDLKSQK VDPQSVIRVD KEFSGVPWNS HDIFQYQDKA YFCHGKFFWR VSFQNEVNKV DHEVNQVDDV GYVTYDLLQC P-HHHHHH
Product Science Overview
MMP-9 is produced by various cell types, including monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, and endothelial cells . It is secreted as an inactive pro-enzyme (proMMP-9) and requires activation in the extracellular space. Activation can occur through various mechanisms, including cleavage by other proteases such as cathepsin K in acidic environments .
- Tissue Remodeling and Wound Healing: MMP-9 plays a crucial role in the degradation of ECM components, facilitating tissue remodeling and wound healing processes .
- Inflammation: MMP-9 is involved in inflammatory responses by modulating the ECM and influencing the behavior of immune cells .
- Tumor Progression: In the context of cancer, MMP-9 contributes to tumor growth, angiogenesis, and metastasis by degrading ECM barriers and promoting cancer cell migration .
- Bone Development and Repair: MMP-9 is essential for bone development and repair. MMP-9 knockout mice exhibit altered growth plate vascularization and ossification during development, as well as delayed bone fracture repair .
Recombinant MMP-9 from mouse is often expressed in NSO cells and is available in a buffered aqueous solution. It is used in various research applications to study its biochemical properties and physiological roles . The recombinant form retains the ability to degrade ECM components and can be activated in vitro to study its enzymatic activity .
