MMP9 Human, Sf9
Description
Definition and Production
MMP9 Human, Sf9 refers to recombinant human MMP-9 expressed in Spodoptera frugiperda (Sf9) insect cells via a baculovirus system . It consists of a 694-amino acid polypeptide (residues 20–707) with an N-terminal hexahistidine (His) tag for purification . The protein has a calculated molecular mass of 77.1 kDa but migrates at 70–100 kDa on SDS-PAGE due to glycosylation .
Table 2: Experimental Uses of MMP9 Human, Sf9
Key Research Findings
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Trimer-Specific Inhibition: A bivalent inhibitor selectively targets MMP-9 trimers (500-fold selectivity over monomers), unexpectedly amplifying neutrophil migration in murine endotoxemia models .
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Regulation by Antibiotics:
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Oxidative Activation: Hypochlorous acid (HOCl) and chloramines activate proMMP-9 at nM–μM concentrations, linking oxidative stress to matrix degradation .
Functional Insights from In Vivo Studies
Product Specs
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Sf9, Baculovirus cells.
APRQRQSTLV LFPGDLRTNL TDRQLAEEYL YRYGYTRVAE MRGESKSLGP ALLLLQKQLS LPETGELDSA TLKAMRTPRC GVPDLGRFQTFEGDLKWHHH NITYWIQNYS EDLPRAVIDD AFARAFALWS AVTPLTFTRV YSRDADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGVVVP TRFGNADGAA CHFPFIFEGR SYSACTTDGR SDGLPWCSTT ANYDTDDRFG FCPSERLYTQ DGNADGKPCQ FPFIFQGQSY SACTTDGRSD GYRWCATTAN YDRDKLFGFC PTRADSTVMG GNSAGELCVF PFTFLGKEYS TCTSEGRGDG RLWCATTSNF DSDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM YPMYRFTEGP PLHKDDVNGI RHLYGPRPEP EPRPPTTTTP QPTAPPTVCP TGPPTVHPSE RPTAGPTGPP SAGPTGPPTA GPSTATTVPL SPVDDACNVN IFDAIAEIGN QLYLFKDGKY WRFSEGRGSR PQGPFLIADK WPALPRKLDS VFEERLSKKL FFFSGRQVWV YTGASVLGPR RLDKLGLGAD VAQVTGALRS GRGKMLLFSG RRLWRFDVKA QMVDPRSASE VDRMFPGVPL DTHDVFQYRE KAYFCQDRFY WRVSSRSELN QVDQVGYVTY DILQCPEDHH HHHH.
Product Science Overview
Matrix Metalloproteinase-9 (MMP-9), also known as Gelatinase B, is a member of the matrix metalloproteinase (MMP) family. These enzymes are zinc and calcium-dependent endopeptidases that play a crucial role in the degradation of the extracellular matrix (ECM) components. The human recombinant form of MMP-9, expressed in Sf9 insect cells, is widely used in research to study its biochemical properties and physiological functions.
MMP-9 is initially synthesized as an inactive zymogen, known as proMMP-9, with a molecular weight of approximately 92 kDa . Activation of proMMP-9 involves the cleavage of its propeptide domain, resulting in the active enzyme with a molecular weight of around 82 kDa . The active form of MMP-9 contains a catalytic domain that is responsible for its enzymatic activity.
MMP-9 plays a significant role in various physiological processes, including:
- Extracellular Matrix Remodeling: MMP-9 degrades various components of the ECM, such as collagen and gelatin, which is essential for tissue remodeling and repair .
- Angiogenesis: MMP-9 regulates the formation of new blood vessels by modulating the ECM and releasing angiogenic factors .
- Wound Healing: MMP-9 is involved in the breakdown of ECM components during the wound healing process, facilitating cell migration and tissue regeneration .
While MMP-9 is vital for normal physiological functions, its dysregulation is associated with several pathological conditions:
- Cancer: Overexpression of MMP-9 is linked to tumor invasion and metastasis, as it degrades the ECM barriers that confine tumor cells .
- Arthritis: MMP-9 contributes to the degradation of cartilage in inflammatory joint diseases such as rheumatoid arthritis .
- Cardiovascular Diseases: Elevated levels of MMP-9 are implicated in the remodeling of blood vessels and the progression of atherosclerosis .
