Recombinant Human MMP-1 Protein Summary
| Description |
A denatured recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 100- 469 of Human MMP-1 Source: E.coli Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSFVLTEGN PRWEQTHLTY RIENYTPDLP RADVDHAIEK AFQLWSNVTP LTFTKVSEGQ ADIMISFVRG DHRDNSPFDG PGGNLAHAFQ PGPGIGGDAH FDEDERWTNN FREYNLHRVA AHELGHSLGL SHSTDIGALM YPSYTFSGDV QLAQDDIDGI QAIYGRSQNP VQPIGPQTPK ACDSKLTFDA ITTIRGEVMF FKDRFYMRTN PFYPEVELNF ISVFWPQLPN GLEAAYEFAD RDEVRFFKGN KYWAVQGQNV LHGYPKDIYS SFGFPRTVKH IDAALSEENT GKTYFFVANK YWRYDEYKRS MDPGYPKMIA HDFPGIGHKV DAVFMKDGFF YFFHGTRQYK FDPKTKRILT LQKANSWFNC RKN |
| Source |
E. coli |
| Protein/Peptide Type |
Recombinant Protein |
| Gene |
MMP1 |
| Purity |
>90%, by SDS-PAGE |
Applications/Dilutions
| Dilutions |
|
| Application Notes |
Denatured protein is most likely not the best option for functional studies. It is better suited for Western Blot (WB) or imaging assays. |
| Theoretical MW |
45 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
| Buffer |
20 mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.4M UREA |
| Preservative |
No Preservative |
| Concentration |
1 mg/ml |
| Purity |
>90%, by SDS-PAGE |
Alternate Names for Recombinant Human MMP-1 Protein
Background
Human interstitial collagenase (matrix metalloproteinase-1, MMP-1), an enzyme whose only known physiologic substrate has heretofore been believed to be the extracellular matrix molecule, collagen. Data indicate that matrix metalloproteinase-1 displays an expanded substrate repertoire that supports the existence of a new interface between connective tissue turnover and serine proteinase inhibitors (1). It has been shown that the MMP-1 functions as a protease agonist of Protease-activated receptors (PAR1) cleaving the receptor at the proper site to generate PAR1-dependent Ca2+ signals and migration. These results demonstrate that MMP-1 in the stromal-tumor microenvironment can alter the behavior of cancer cells through PAR1 to promote cell migration and invasion (2). It has also been suggested that increased levels of MMP-1 due to tobacco smoking plays a major role in the aging process of skin since MMP-1 degrades collagen, which accounts for at least 70% of the dry weight of dermis. Significantly more MMP-1 has been detected in the skin of smokers than non-smokers whereas no difference was seen for the tissue inhibitor of metalloproteinases 1 (3).
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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