MMP9 Mouse

AW743869, Matrix metalloproteinase-9, 92 kDa type IV collagenase, Gelatinase B, GELB, Mmp9, MANDP2, B/MMP, B/MMP9, Clg4, Clg4b, Gel B, MMP-9, pro-MMP-9, 92 kDa gelatinase.

MMP9 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-730 a.a) containing a total of 717 amino acids, having a molecular mass of 79.3kDa.
MMP9 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

HEK293 Cells. 

MMP9 protein solution (1mg/ml) containing 10% glycerol, 20mM Tris-HCl (pH 7.5), 1mM CaCl2 and 0.1M NaCl.

Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.

Greater than 90.0% as determined by SDS-PAGE.

Specific activity is greater than 1,500 pmol/min/ug and is defined by the amount of enzyme that cleaves 1pmole of  Mca-PLGLDpa-AR-NH2 per minute at pH 7.5 at 37˚C.

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 PHHHHHH.

SDS

The MMP9 mouse recombinant, a variant of the matrix metalloproteinase 9 enzyme, has emerged as a crucial focus of biomedical research due to its diverse biological functions and potential implications in various physiological and pathological processes. Matrix metalloproteinase 9 (MMP9) is a key enzyme involved in extracellular matrix remodeling, cell migration, and tissue homeostasis. The MMP9 mouse recombinant, generated through recombinant DNA technology, offers a valuable tool for investigating the molecular characteristics and biological roles of this enzyme.

Understanding the molecular characteristics of MMP9 is vital to unravel its functional significance. MMP9 belongs to the matrix metalloproteinase family, characterized by their ability to degrade various components of the extracellular matrix. MMP9 exhibits unique structural features, including a catalytic domain, a hemopexin-like domain, and a prodomain that regulates its activation. These characteristics contribute to the complexity of MMP9 and its involvement in multiple physiological and pathological processes.

MMP9 plays diverse roles in different biological contexts. It is involved in tissue remodeling processes, such as embryogenesis, wound healing, and tissue repair. Additionally, MMP9 participates in inflammatory responses, immune cell recruitment, and angiogenesis. The precise mechanisms underlying these functions are still being elucidated, highlighting the need for further investigation.

The MMP9 mouse recombinant offers exciting prospects for research and therapeutic applications. By utilizing this recombinant protein, scientists can investigate the role of MMP9 in disease progression, explore its interactions with other molecules, and potentially develop targeted therapies. MMP9 has been implicated in various diseases, including cancer metastasis, cardiovascular disorders, and neurodegenerative conditions, making it a promising candidate for therapeutic interventions.

This research aims to provide a comprehensive analysis of the MMP9 mouse recombinant, focusing on its molecular characteristics, biological roles, and potential therapeutic implications. By shedding light on the intricate nature of MMP9, we aim to contribute to a deeper understanding of its functional significance and pave the way for future research and therapeutic advancements.