AV33090
Anti-MMP9 antibody produced in rabbit
IgG fraction of antiserum
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Product Name
Anti-MMP9 antibody produced in rabbit, IgG fraction of antiserum
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
78 kDa
species reactivity
human, dog, mouse, guinea pig, horse, bovine, sheep, rat, rabbit
concentration
0.5 mg - 1 mg/mL
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MMP9(4318)
Other Notes
Synthetic peptide located within the following region: VAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTR
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Rabbit polyclonal anti-MMP9 antibody is used to tag matrix metalloproteinase-9/gelatinase B for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques. It is used as a probe to determine the presence and roles of matrix metalloproteinase-9/gelatinase B in processe such as synaptic plasticity.
Biochem/physiol Actions
Proteins of the matrix metalloproteinase (MMP) family are 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, such as arthritis and metastasis. Most MMP′s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by MMP9 degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Matrix metalloproteinase-9/gelatinase B (MMP-9), a member of the matrix metalloproteinase (MMP) family, is involved in the breakdown of extracellular matrix giving it a role in normal physiological processes such as embryonic development, tissue remodeling, wound repair, vascularization and inflammatory response. MMP-9 is involved in synaptic plasticity. MMP-9 functions in modulating hippocampal synaptic physiology and plasticity.
Immunogen
Synthetic peptide directed towards the N terminal region of human MMP9
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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Prashant Nighot et al.
American journal of physiology. Gastrointestinal and liver physiology, 309(12), G988-G997 (2015-10-31)
Recent studies have implicated a pathogenic role for matrix metalloproteinases 9 (MMP-9) in inflammatory bowel disease. Although loss of epithelial barrier function has been shown to be a key pathogenic factor for the development of intestinal inflammation, the role of
Perle Latré De Laté et al.
Cellular microbiology, 21(3), e12973-e12973 (2018-11-10)
Constitutive c-Jun N-terminal kinase (JNK) activity characterizes bovine T and B cells infected with Theileria parva, and B cells and macrophages infected with Theileria annulata. Here, we show that T. annulata infection of macrophages manipulates JNK activation by recruiting JNK2 and
K Nagaoka et al.
Oncogene, 35(22), 2893-2901 (2015-09-29)
In mouse mammary epithelial cells, cytoplasmic polyadenylation element binding protein 1 (CPEB1) mediates the apical localization of ZO-1 mRNA, which encodes a critical tight junction component. In mice lacking CPEB1 and in cultured cells from which CPEB has been depleted
Gokhan Gundogdu et al.
International journal of impotence research, 36(3), 269-274 (2023-02-14)
Peyronie's disease (PD) is a debilitating pathology which is associated with penile curvature and erectile dysfunction due to the formation of fibrotic plaques in the penile tunica albuginea. In the present study, we developed a novel rabbit model of PD
Mirel-Adrian Popa et al.
Journal of molecular endocrinology, 60(1), 1-15 (2017-12-17)
The use of mesenchymal stem cells (MSC) as a therapeutic tool in cardiovascular diseases is promising. Since androgens exert some beneficial actions on the cardiovascular system, we tested our hypothesis that this hormone could promote MSC-mediated repair processes, also. Cultured
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