Search
Gibco
Human MMP-2 Recombinant Protein, PeproTech®
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.promotions']}}
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.viewpromo']}}
{{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.promocode']}}: {{promo.promoCode}} {{promo.promoTitle}} {{promo.promoDescription}}. {{$productOrderCtrl.translations['antibody.pdp.commerceCard.promotion.learnmore']}}
Additional Information:
{{banner.description}}
Product Details
420-02-1MG
Applications
Tested Dilution
Publications
Product Specifications
Published species
Human,
Mouse
Expression System
E. coli
Class
Recombinant
Type
Protein
Conjugate
Form
Lyophilized
Storage conditions
-20°C
Shipping conditions
Ambient
Product Specific Information
420-02-1MG will be provided as 2 x 500 µg (420-02-500UG).
Recombinant Human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis
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.
Disclaimer
Clicking the images or links will redirect you to a website hosted by BenchSci that provides third-party scientific content. Neither the content nor the BenchSci technology and processes for selection have been evaluated by us; we are providing them as-is and without warranty of any kind, including for use or application of the Thermo Fisher Scientific products presented.
We're here to help
Get expert recommendations for common problems or connect directly with an on staff expert for technical assistance related to applications, equipment and general product use.
Contact tech support