Matrix Metalloproteinase-9 (MMP9) Antibody

Descripción

MMP9 antibody detects endogenous levels of total MMP9. MMP9 May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. Belongs to the peptidase M10A family. Activated by 4-aminophenylmercuric acetate and phorbol ester. Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.

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

immunogen target

Matrix Metalloproteinase-9 (MMP9)

host

Rabbit

conjugation

Unconjugated

form

Liquid

tested applications

WB, IHC

purification

Purified by affinity chromatography.

buffer

PBS, pH 7.4, 150 mM NaCl, 0.02% sodium azide and 50% glycerol.

size 1

10 µl

size 2

20 µl

size 3

100 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

note

This product is for research use only.

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