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          • Proteins & Peptides ›
          • MMP2 Proteins
          The PeproTech website has now moved to Thermofisher.com. All orders for PeproTech products must be placed on thermofisher.com or offline via phone, fax, email, or distributor partner. For any questions, please contact PeproTech.CustomerService@thermofisher.com

          Gibco

          Human MMP-2 Recombinant Protein, PeproTech®

          7 References
          View all (2) MMP2 proteins
          Datasheet
          Tech Support
          Datasheet
          Tech Support

          Cite Human MMP-2 Recombinant Protein, PeproTech®

          • Testing Data (1)
          Human MMP-2 Protein in Functional Assay (Functional)
          Group 53 Created with Sketch.
          Human MMP-2 Protein in Functional Assay (Functional)
          Group 53 Created with Sketch.

          FIGURE: 1 / 1

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          Human MMP-2 Protein (420-02-100UG) in Functional

          Bioassay analysis of Human MMP-2 Recombinant Protein, PeproTech® (Product # 420-02-1MG). {{ $ctrl.currentElement.advancedVerification.fullName }} validation info. View more
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          Human MMP-2 Protein in Functional Assay (Functional)

          Product Details

          420-02-100UG

          Applications
          Tested Dilution
          Publications

          Functional Assay (Functional)

          Assay-dependent
          -

          In vitro Assay (IV)

          -
          View 5 publications 5 publications

          Miscellaneous PubMed (Misc)

          -
          View 2 publications 2 publications
          Product Specifications

          Species

          Human

          Published species

          Human, Mouse

          Expression System

          E. coli

          Amino acid sequence

          MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTLGEG QVVRVKYGNA DGEYCKFPFL FNGKEYNSCT DTGRSDGFLW CSTTYNFEKD GKYGFCPHEA LFTMGGNAEG QPCKFPFRFQ GTSYDSCTTE GRTDGYRWCG TTEDYDRDKK YGFCPETAMS TVGGNSEGAP CVFPFTFLGN KYESCTSAGR SDGKMWCATT ANYDDDRKWG FCPDQGYSLF LVAAHEFGHA MGLEHSQDPG ALMAPIYTYT KNFRLSQDDI KGIQELYGAS PDIDLGTGPT PTLGPVTPEI CKQDIVFDGI AQIRGEIFFF KDRFIWRTVT PRDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN EYWIYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM DPGFPKLIAD AWNAIPDNLD AVVDLQGGGH SYFFKGAYYL KLENQSLKSV KFGSIKSDWL GC

          Molecular weight

          62 kDa

          Class

          Recombinant

          Type

          Protein

          Purity

          ≥ 98% by SDS-PAGE gel and HPLC analyses.

          Endotoxin concentration

          <1 EU/µg

          Activity

          MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 ug/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.

          Conjugate

          Unconjugated Unconjugated Unconjugated

          Form

          Lyophilized

          Purification

          purified

          Contains

          no preservative

          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.

          Bioinformatics

          Protein Aliases: 72 kDa gelatinase; 72 kDa type IV collagenase; CLG 4A; Collagenase; collagenase type IV-A; Gelatinase A; Gelatinase alpha; Mat; matrix metallo protease; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Matrix metalloproteinase-2; matrix metalloproteinase-II; MMP; MMP-2; MMPs; neutrophil gelatinase; Progelatinase A; TBE-1; TBE1

          View more View less

          Gene Aliases: CLG4; CLG4A; MMP-2; MMP-II; MMP2; MONA; TBE-1

          View more View less

          UniProt ID: (Human) P08253

          View more View less

          Entrez Gene ID: (Human) 4313

          View more View less

          It has to be done as per old AB suggested Products section.
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