Abcam, ab58803, Anti-MMP9 antibody [56-2A4]

Size: 50µg
Anti-MMP9 antibody [56-2A4] (ab58803) is a mouse monoclonal antibody detecting MMP9 in Western Blot, IHC-P, IHC-Fr, ICC/IF . Suitable for Guinea pig, Human, Mouse, Rabbit, Rat . - Over 110 publications - Trusted since 2007
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:56-2A4,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:No,
Reacts with:Human, Rabbit, Guinea pig, Rat, Mouse,
Applications:IHC-P, IHC-Fr, WB, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human MMP9 aa 600-650. The exact immunogen used to generate this antibody is proprietary information.P14780,
Specificity:Recognizes the ~92 kDa latent and the ~83 kDa active forms of MMP9.Does not react with MMP1, MMP2, MMP3 or MMP13.The antibody recognizes precursor (92 kDa) and active (83 kDa) forms of human and guinea pig MMP-9.

Product details:
What is this antibody validated in?
Anti-MMP9 antibody [56-2A4] (ab58803) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Immunohistochemistry (IHC-P), Immunohistochemistry (IHC-Fr), Immunocytochemistry/immunofluorescence (ICC/IF) in Guinea pig, Human, Mouse, Rabbit, Rat samples.
What is the molecular weight of MMP9?
Anti-MMP9 [56-2A4] (ab58803) specifically detects a band for MMP9 (UniProt: P14780) at a molecular weight of 78kDa.
Trusted by the scientific community
Anti-MMP9 [56-2A4] (ab58803) was first used in a scientific publication in 2007 and has been cited over 110 times in peer-reviewed journals.
Reviewed by scientists
Anti-MMP9 [56-2A4] (ab58803) has over 5 independent reviews from customers.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-Is purified., Storage buffer-pH: 7Preservative: 0.1% Sodium azideConstituents: 1.64% Sodium phosphate, 0.1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The MMP-9 protein also known as matrix metalloproteinase-9 or gelatinase B functions as an enzyme involved in the breakdown of extracellular matrix proteins. It consists of a zinc ion at its active site and facilitates the degradation of type IV and V collagens fibronectin and elastin. MMP-9 has a molecular weight of approximately 92 kDa and is expressed in a variety of tissues including the liver lungs and immune cells. This enzyme can exist in monomer and dimer forms with its activity regulated by tissue inhibitors of metalloproteinases (TIMPs).
Biological function summary
Matrix metalloproteinase-9 profoundly influences tissue remodeling inflammation and angiogenesis. It does not form part of a larger protein complex but interacts closely with substrates in the extracellular matrix. MMP-9 plays important roles in processes such as embryogenesis reproduction and wound healing through the remodeling of surrounding tissues. The MMP-9 protein is often measured using assays like ELISA or analyzed via techniques such as Western blotting to determine its expression levels and activity in different biological contexts.
Pathways
MMP-9 participates in the matrix metalloproteinase pathway and the NF-kB signaling pathway. These pathways are essential in orchestrating processes such as tissue remodeling and inflammatory responses. MMP-9 acts alongside other matrix metalloproteinases including MMP-2 and is regulated by factors like cytokines growth factors and hormones ensuring the precision of extracellular matrix degradation during physiological processes.
Matrix metalloproteinase-9 has associations with cancer invasion and metastasis as well as chronic inflammatory diseases like rheumatoid arthritis. In cancer upregulated MMP-9 expression aids tumor cells in breaching the basement membrane facilitating metastasis. The disorder-associated pathways often involve interactions with proteins like vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta). Understanding MMP-9's role in these conditions can contribute to developing targeted therapies that inhibit its activity potentially mitigating disease progression.