Product Name:
MMP9
Product Number:
ab-nn292-1
Target Full Name: Matrix metalloproteinase-9
Target Alias: MMP-9; CLG4B; 82kDa matrix metalloproteinase-9; collagenease type 4 beta; GELB ; Macrophage gelatinase; MANDP2; Type V collagenase; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B
Product Type Specific: Metaloproteinase pan-specific antibody
Antibody Code: NN292-1
Antibody Target Type: Pan-specific
Protein UniProt: P14780
Protein SigNET: MMP9
Antibody Type: Monoclonal
Antibody Host Species: Mouse
Antibody Ig Isotype Clone: IgG2a
Antibody Immunogen Source: Fusion protein of full length rat MMP9 (Uniprot ID. P50282)
Antibody Immunogen Description: Corresponds to amino acid residues M1-P708.
Production Method: Protein G purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1 mg/ml
Storage Buffer: Phosphate buffered saline pH7.4, 50% glycerol, 0.09% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | Immunohistochemistry | Immunoprecipitation | FCM
Antibody Dilution Recommended: WB (1:1000); optimal dilutions for assays should be determined by the user.
Antibody Potency: Detects a ~92 kDa protein and ~82 kDa protein (pro and active forms).
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Rat | Mouse.
Antibody Positive Control: 1 µg/ml of SMC-396 was sufficient for detection of MMP9 in 20 µg of COS-1 cells (lysate) transfected with human MMP9 by colorimetric immunoblot analysis using goat anti-mouse IgG:HRP as the secondary antibody.
Antibody Specificity: Very high
Scientific Background: MMP9 (Matrix metalloproteinase 9; gelatinae B) is a 92 kDa zinc-dependent enzyme that breaks down extracellular matrix (ECM) components like gelatin and type IV and. V collagen, and elastin. It is involved in the breakdown of extracellular matrix in normal physiological processes such as embryonic development, reproduction and tissue remodeling, as well as in disease processes like arthritis and metastasis (1). Among the family members, MMP-2, MMP-3, MMP-7 and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumour invasion, angiogenesis, carcinogenesis and apoptosis (2-4). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5). It is comprised of an N-terminal pro-domain, catalytic domain, and a C-terminal hemopexin-like domain. It feature a three fibronectin type II repeats embedded within its catalytic domain, which increases its binding affinity for gelatin. It is activated by the cleavage of a cysteine-switch motif (PRCGVPD) in its pro-domain, reducing it from a 92 kDa latent form to an 82 kDa active enzyme. It regulates neutrophil migration across the basement membrane and activates pro-inflammatory cytokines like IL-1β. It facilitates new blood vessel formation by activating VEGF and promoting endothelial cell recruitment. Elevated levels of MMP9 are linked to chronic inflammation, cardiovascular diseases (like aortic aneurysms), and neuroinflammation (e.g., blood-brain barrier dysfunction). High levels of MMP9 are associated with cancer metastasis and invasion, as it breaks down collagen to allow tumour cells to migrate (2). This description may include information annotated by UniProt and/or Google AI.