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Gibco
Human MMP-2 Recombinant Protein, PeproTech®
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Product Details
420-02-10UG
Applications
Tested Dilution
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
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 precursor; 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; unnamed protein product
Gene Aliases: CLG4; CLG4A; MMP-2; MMP-II; MMP2; MONA; TBE-1
UniProt ID: (Human) P08253
Entrez Gene ID: (Human) 4313
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