Thermo Fisher Scientific MMP2 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:2,000

-

Immunohistochemistry (IHC)

-

View 1 publication 1 publication

Immunohistochemistry (Paraffin) (IHC (P))

1:50-1:200

-

Immunocytochemistry (ICC/IF)

1:100-1:500

-

Product Specifications

Species Reactivity

Human, Mouse, Non-human primate, Rat

Published species

Mouse

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

A synthesized peptide derived from human MMP2(Accession P08253), corresponding to amino acid residues D618-C660. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:MMP2,uniProtId:P08253-1,ncbiNodeId:9606,antigenRange:618-660,antigenLength:660,antigenImageFileName:PA5-115583_MMP2_P08253-1_Rabbit.svg,antigenImageFileNamePDP:PA5-115583_MMP2_P08253-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Affinity chromatography

Storage buffer

PBS with 50% glycerol

Contains

0.02% sodium azide

Storage conditions

-20°C

Shipping conditions

Wet ice

RRID

AB_2900218

Product Specific Information

Antibody detects endogenous levels of total MMP2.

Target Information

MMP (matrix metalloproteinase) are proteolytic enzymes capable of degrading connective tissue components. MMP have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). MMPa and TIMPs play a significant role in regulating angiogenesis. MMP2 is synthesized as a 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids, and contains the basic structure of propeptide, catalytic, and hemopexin domains. The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. Functionally, MMP2 is involved in tissue remodeling. Mutations in MMP-2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms of MMP-2 have been found.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.