AV33090
Anti-MMP9 antibody produced in rabbit
IgG fraction of antiserum
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About This Item
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
IgG fraction of antiserum
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Poids mol.
78 kDa
Espèces réactives
human, dog, mouse, guinea pig, horse, bovine, sheep, rat, rabbit
Concentration
0.5 mg - 1 mg/mL
Technique(s)
immunohistochemistry: suitable
western blot: suitable
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... MMP9(4318)
Catégories apparentées
Description générale
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.
Immunogène
Synthetic peptide directed towards the N terminal region of human MMP9
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.
Actions biochimiques/physiologiques
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.
Séquence
Synthetic peptide located within the following region: VAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTR
Forme physique
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Clause de non-responsabilité
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.
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
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
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
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
Qiang Zhang et al.
Chinese medical journal, 135(9), 1076-1086 (2022-02-23)
Fibrosis in the peripheral airways contributes to airflow limitation in patients with chronic obstructive pulmonary disease (COPD). However, the key proteins involved in its development are still poorly understood. Thus, we aimed to identify the differentially expressed proteins (DEPs) between
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