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anti- MMP9 antibody
proveedor
FineTestreference
FNab05247Tested Applications
ELISA, WB, IHCreactivity
human,mouse,ratstatus
RUOclonality
polyclonalDescripción
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 this gene 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.
Background
MMPs are secreted by diverse connective tissue and pro-inflammatory cells. Typically, these enzymes exhibit minimal expression under normal physiological circumstances. MMPs assume a pivotal role in various cellular processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and immunity. They share a common domain structure, consisting of three key components. First is the pro-peptide, which requires removal to activate the enzyme. Next, there is the catalytic domain, featuring a cysteine switch, where a cysteine residue interacts with zinc, and the haemopexin-like C-terminal domain is linked to the catalytic domain via a flexible hinge region. MMP-9, alternatively known as 92 kDa type IV collagenase, 92 kDa gelatinase, or gelatinase B (GELB), belongs to the zinc-metalloproteinases within the Matrixin family. In humans, the MMP-9 gene is responsible for encoding this enzyme. MMP-9's substrates include gelatin and collagen types IV and V. This gelatinase, MMP-9, has been associated with various medical conditions, including the development of atherosclerosis, chronic obstructive pulmonary disease (COPD), tumor formation, metastasis, and wound repair
Background
MMPs son secretadas por diversos tejidos conectivos y células proinflamatorias. Normalmente, estas enzimas exhiben una expresión mínima en circunstancias fisiológicas normales. Las MMP asumen un papel fundamental en diversos procesos celulares, incluida la proliferación, migración, diferenciación, angiogénesis, apoptosis e inmunidad celular. Comparten una estructura de dominio común, que consta de tres componentes clave. El primero es el propéptido, que requiere eliminación para activar la enzima. A continuación, está el dominio catalítico, que presenta un interruptor de cisteína, donde un residuo de cisteína interactúa con el zinc, y el dominio C-terminal similar a hemopexina está unido al dominio catalítico a través de una región bisagra flexible. MMP-9, también conocida como colagenasa tipo IV de 92 kDa, gelatinasa de 92 kDa o gelatinasa B (GELB), pertenece a las metaloproteinasas de zinc dentro de la familia Matrixin. En humanos, el gen MMP-9 es el responsable de codificar esta enzima. Los sustratos de MMP-9 incluyen gelatina y colágeno de tipos IV y V. Esta gelatinasa, MMP-9, se ha asociado con diversas afecciones médicas, incluido el desarrollo de aterosclerosis, enfermedad pulmonar obstructiva crónica (EPOC), formación de tumores, metástasis y reparación de heridas
Características del producto
category
Primary Antibodies
clonality
polyclonal
reactivity
human,mouse,rat
immunogen target
matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
host
Rabbit
isotype
IgG
conjugation
Unconjugated
form
liquid
tested applications
ELISA, WB, IHC
observerd MW
68 kDa
purity
≥95% as determined by SDS-PAGE
purification
Immunogen affinity purified
recommended dilution
WB: 1:200 - 1:500; IHC: 1:100 - 1:200
size 1
100µg
storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3 , -20℃ for 12 months (Avoid repeated freeze / thaw cycles.)
or code
MMP9
alias
GELB,CLG4B,MMP-9,MANDP2,92 kDa type IV collagenase, Gelatinase B
uniprot id
note
This product is for research use only.
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