Recombinant Human MMP2
proveedor
FineTestreference
P4588Tested Applications
Western Blot,ELISAreactivity
status
RUOclonality
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. Matrix metalloproteinase-2 (MMP-2), also referred to as gelatinase A, is an enzyme encoded by the MMP2 gene in humans. MMP-2 exhibits a wide range of substrates, including gelatin, collagen types I, II, III, IV, Vii, and X. It has been implicated in various aspects of cancer, including therapy, angiogenesis, and cell signaling. Among its aliases are CLG4, Gelatinase A, 72kDa Gelatinase, 72kDa Type IV Collagenase, Matrix Metalloproteinase-II, and Collagenase Type IV-A.
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-2, también conocida como gelatinasa A, es una enzima codificada por el gen MMP2. En humanos. MMP-2 exhibe una amplia gama de sustratos, incluidos gelatina, colágeno de tipo I, II, III, IV, Vii y X. Se ha implicado en diversos aspectos del cáncer, incluida la terapia, la angiogénesis y la señalización celular. Entre sus alias se encuentran CLG4, Gelatinasa A, Gelatinasa de 72 kDa, Colagenasa Tipo IV de 72 kDa, Metaloproteinasa de Matriz-II y Colagenasa Tipo IV-A.
Características del producto
immunogen target
109-660
category
Proteins and Peptides
origin
Human
size 1
50μg
size 2
200μg
size 3
1mg
host
E.Coli
form
Lyophilized from a 0.2um filtered solution in PBS with 5% trehalose, pH7.4
expression
Recombinant
purity
Greater than 95% by SDS-PAGE gel analyses
purification
His tag
storage
-20°C for 12 months as lyophilized;2-8°C for 1 month under sterile conditions after reconstitution
uniprot id
P08253
buffer
Reconstitute with Sterile distilled water
availability
3-4 weeks
note
This product is for research use only.
alias
72 kDa gelatinase, 72kD type IV collagenase, CLG 4, CLG 4A, CLG4, CLG4A, Collagenase Type 4 alpha, Collagenase type IV A, Gelatinase A, Gelatinase alpha, Gelatinase neutrophil, Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase, Matrix Metalloproteinase 2, Matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), Matrix metalloproteinase II
observerd MW
60.6 kDa
status
RUO
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