Thermo Fisher Scientific MMP2 Monoclonal Antibody (4D1E2)

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:2,000

-

ELISA (ELISA)

1:10,000

-

Product Specifications

Species Reactivity

Human, Mouse

Host/Isotype

Mouse / IgG1

Class

Monoclonal

Type

Antibody

Clone

4D1E2

Immunogen

Purified recombinant fragment of human MMP2 (amino acids: 242-396) expressed in E. Coli. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:MMP2,uniProtId:P08253-1,ncbiNodeId:9606,antigenRange:242-396,antigenLength:660,antigenImageFileName:MA5-17122_MMP2_P08253-1_House_mouse.svg,antigenImageFileNamePDP:MA5-17122_MMP2_P08253-1_House_mouse_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Protein G

Storage buffer

PBS

Contains

0.05% sodium azide

Storage conditions

Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.

Shipping conditions

Ambient (domestic); Wet ice (international)

RRID

AB_2538593

Product Specific Information

MA5-17122 targets MMP2 in indirect ELISA and WB applications and shows reactivity with Human samples.

The MA5-17122 immunogen is purified recombinant fragment of human MMP2 (amino acids: 242-396) expressed in E. Coli.

MA5-17122 detects MMP2 which has a predicted molecular weight of approximately 73.8kDa.

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.