Gibco™ Human MMP-2 Recombinant Protein, PeproTech®

Description

Recombinant Protein

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

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.

Specifications

• Accession Number: P08253
• For Use With (Application): Functional Assay
• Formulation: protein with no preservative
• Gene ID (Entrez): 4313
• Molecular Weight (g/mol): 62 kDa
• Name: Human MMP-2
• Quantity: 10 μg
• Source: E. coli
• Regulatory Status: RUO
• Endotoxin Concentration: <1 EU/ μg
• Gene Alias: 72 kDa gelatinase; 72 kDa type IV collagenase; 72 kDa type IV collagenase isoform a preproprotein; 72 kD gelatinase; 72 kD type IV collagenase; 72 kDa gelatinase; 72 kDa type IV collagenase; CLG 4 A; CLG4; CLG4A; Collagenase; collagenase type IV-A; endopeptidase; GelA; gelatinase A; Gelatinase alpha; Mat; matrix metallo protease; matrix metallopeptidase 2; matrix metallopeptidase 2 (gelatinase A, 72 kDa gelatinase, 72 kDa type IV collagenase); matrix metalloprotease 2; matrix metalloproteinase; matrix metalloproteinase 2; matrix metalloproteinase 2 (72 KDa type IV collagenase); matrix metalloproteinase 2 (gelatinase A, 72 kDa gelatinase, 72 kDa type IV collagenase); matrix metalloproteinase-2; matrix metalloproteinase-II; MMP; MMP2; MMP-2; MMP-2 protein; MMP-II; MMPs; MONA; neutrophil gelatinase; PEX; prepro-72 kDa matrix metalloproteinase; Progelatinase A; TBE1; TBE-1; wu:fa99h12; wu:fk89d01
• Common Name: MMP2
• Gene Symbol: MMP2
• Biological 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
• Recombinant: Recombinant
• 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
• Content And Storage: -20°C
• Expression System: E. coli
• Form: Lyophilized
• Purity or Quality Grade: ≥ 98% by SDS-PAGE gel and HPLC analyses.