MMP7 Protein, Human, Recombinant (hFc 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.
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 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
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.
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 the 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. Besides, matrilysin is also identified as a mediator of pulmonary fibrosis and a potential therapeutic target.
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.
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