MMP9 Rat
HEK293 Cells.
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Sterile filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
MMP9 Rat produced in HEK293 cells is a single, glycosylated polypeptide chain containing 695 amino acids (20-708 a.a.) and having a molecular mass of 77.2kDa. MMP9 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
HEK293 Cells.
APHQRQPTYV VFPRDLKTSN LTDTQLAEDY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS ETLKAIRSPR CGVPDVGKFQ TFEGDLKWHH HNITYWIQSY TEDLPRDVID DSFARAFAVW SAVTPLTFTR VYGLEADIVI QFGVAEHGDG YPFDGKDGLL AHAFPPGPGI QGDAHFDDDE LWSLGKGAVV PTYFGNANGA PCHFPFTFEG RSYLSCTTDG RNDGKPWCGT TADYDTDRKY GFCPSENLYT EHGNGDGKPC VFPFIFEGHS YSACTTKGRS DGYRWCATTA NYDQDKLYGF CPTRADVTVT GGNSAGEMCV FPFVFLGKQY STCTGEGRSD GRLWCATTSN FDADKKWGFC PDQGYSLFLV AAHEFGHALG LDHSSVPEAL MYPMYHYHED SPLHEDDIKG IQHLYGRGSK PDPRPPATTA AEPQPTAPPT MCPTAPPMAY PTGGPTVAPT GAPSPGPTGP PTAGPSEAPT ESSTPVDNPC NVDVFDAIAD IQGALHFFKD GRYWKFSNHG GSQLQGPFLI ARTWPALPAK LNSAFEDPQS KKIFFFSGRK MWVYTGQTVL GPRSLDKLGL GSEVTLVTGL LPRRGGKALL ISRERIWKFD LKSQKVDPQS VTRLDNEFSG VPWNSHNVFH YQDKAYFCHD KYFWRVSFHN RVNQVDHVAY VTYDLLQCPH HHHHH.
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 capable of degrading various components of the extracellular matrix (ECM), such as collagen, elastin, and proteoglycans . MMP-9 is particularly notable for its role in both physiological and pathological processes, including tissue remodeling, inflammation, and cancer metastasis .
MMP-9 is initially produced as an inactive zymogen (proMMP-9) that requires activation to become enzymatically functional . The activation process involves the cleavage of the pro-domain, which masks the catalytic site of the enzyme. This cleavage can be mediated by other proteases, oxidative modifications, or conformational changes due to substrate binding .
MMP-9 plays a crucial role in various biological processes:
- Tissue Remodeling: MMP-9 is involved in the degradation of ECM components, facilitating tissue remodeling and repair .
- Inflammation: MMP-9 is upregulated during inflammatory responses and contributes to the migration of leukocytes to the site of inflammation by degrading basement membrane components .
- Neuroinflammation and Cerebral Ischemia: MMP-9 is actively involved in blood-brain barrier disruption following cerebral ischemia and neuroinflammation .
- Synaptic Plasticity and Memory: In the brain, MMP-9 is required for hippocampal late-phase long-term potentiation (L-LTP) and memory formation .
MMP-9 is implicated in several pathological conditions:
- Cancer: MMP-9 facilitates cancer cell invasion and metastasis by degrading ECM barriers .
- Cardiovascular Diseases: MMP-9 contributes to the atherogenic environment of the vessel wall and is involved in the regulation of cytokine production and macrophage function .
- Bone Diseases: MMP-9 plays a regulatory role in osteoclastogenesis, linking cardiovascular diseases and bone disorders in high-fat diet-fed rats .
Recombinant MMP-9 (Rat) is a laboratory-produced version of the enzyme, often used in research to study its functions and interactions. The recombinant form allows for controlled experiments to understand the enzyme’s role in various biological and pathological processes.
