Thermo Fisher Scientific MMP2 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:1,000

-

Immunohistochemistry (IHC)

1:100

-

Immunocytochemistry (ICC/IF)

15 µg/mL

-

ELISA (ELISA)

1:10,000-1:50,000

-

Product Specifications

Species Reactivity

Human

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Anti-MMP2 antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to an internal portion of human MMP2 conjugated to Keyhole Limpet Hemocyanin (KLH).

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Affinity chromatography

Storage buffer

0.02M potassium phosphate, pH 7.2, with 0.15M NaCl

Contains

0.01% sodium azide

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Ambient (domestic); Wet ice (international)

Product Specific Information

Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.

This affinity purified antibody is directed against human MMP2. A BLAST analysis was used to suggest cross-reactivity with the antigen based on 100% homology with the immunizing sequence to mouse, rat, bovine,and Oryctolagus cuniculus.

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.