MMP7 Protein, Human, Recombinant (Fc Tag)

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MMP7 Protein, Human, Recombinant (Fc Tag): Product Information

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Testing in progress
Protein Construction
A DNA sequence encoding the active form of human MMP7 (NP_002414.1) (Tyr 95-Lys 267) was expressed with the fused Fc region of human IgG1 at the N-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Glu 20
Molecule Mass
The recombinant human Fc/MMP7 chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 410 amino acids and predicts a molecular mass of 45.8 kDa. As a result of glycosylation, the rh Fc/MMP7 monomer migrates as an approximately 55 kDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

MMP7 Protein, Human, Recombinant (Fc Tag): Images

MMP7 Protein, Human, Recombinant (Fc Tag): Alternative Names

MMP-7 Protein, Human; MPSL1 Protein, Human; PUMP-1 Protein, Human

MMP7 Background Information

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological and pathological processes such as morphogenesis, differentiation, angiogenesis, tissue remodeling, and tumor invasion. MMPs are synthesized as pro-enzymes and converted to active form by extracellular proteinases. MMP7, also referred to as matrilysin, is the smallest member of the MMP family and differs from other MMP members in that it lacks the C-terminal hemopexin-like domain. MMP7 is produced primarily by mucosal epithelia, and is capable of degrading various ECM proteins including proteoglycans, fibronectin, elastin and casein. This enzyme serves essential functions in both innate defense and wound healing, and appears to be one of the most important MMPs in human colon cancers. It has been reported that MMP7 contributes to tumor malignancy probably by cleaving cell surface proteins such as Fas ligand, degradation of IgG or inducing E-cadherin-mediated cell aggregation. In addition, matrilysin is also identified as a mediator of pulmonary fibrosis and a potential therapeutic target.
Full Name
matrix metallopeptidase 7
References
  • Muller D., et al.,(1988), The collagenase gene family in humans consists of at least four members. Biochem. J. 253:187-192.
  • Marti H.P., et al., (1992), Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1.Biochem. J. 285:899-905.
  • Gaire M., et al.,(1994), Structure and expression of the human gene for the matrix metalloproteinase matrilysin.J. Biol. Chem. 269:2032-2040.
  • DNA Enzyme-Decorated DNA Nanoladders as Enhancer for Peptide Cleavage-Based Electrochemical Biosensor
    Author
    Kou, BB;Zhang, L;Xie, H;Wang, D;Yuan, YL;Chai, YQ;Yuan, R;
    Year
    2016
    Journal
    ACS Appl Mater Interfaces
    Application
    binding (peptide)
  • Amperometric Biosensor of Matrix Metalloproteinase-7 Enhanced by Pd-Functionalized Carbon Nanocomposites
    Author
    Wei, Z;Wang, H;Ma, Z;Han, H;
    Year
    2018
    Journal
    Nanoscale Res Lett
    Application
    enzyme
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