Matrix Metalloproteinase-9 (MMP9) Antibody

Descripción

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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. 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.

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

clonality

Polyclonal

reactivity

Human, Mouse

immunogen target

Matrix Metalloproteinase-9 (MMP9)

host

Rabbit

conjugation

Unconjugated

form

Liquid

tested applications

ELISA, WB, IHC

purification

Purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.

buffer

PBS containing 0.09% sodium azide.

size 1

80 µl

size 2

400 µl

storage

Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

or code

MMP9

dry ice

availability

Shipped within 5-10 working days.

alias

GELB,CLG4B,MMP-9,MANDP2,92 kDa type IV collagenase, Gelatinase B

uniprot id

https://www.uniprot.org/uniprotkb/P14780

NCBI accession

NP_004985.2

note

This product is for research use only.

Quizá le pueda interesar