The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
MMP-8 cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information
**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**
MMP-8 cDNA ORF Clone in Cloning Vector, Human: Synonyms
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 processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M1A family. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumor may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.
matrix metallopeptidase 8
Hasty K.A., et al.,(1990), Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J. Biol. Chem. 265:11421-11424.
Blaeser J., et al., (1991), Mercurial activation of human polymorphonuclear leucocyte procollagenase.Eur. J. Biochem. 202:1223-1230.
Blaeser J., et al.,(1991), Mercurial activation of human polymorphonuclear leucocyte procollagenase. Eur. J. Biochem. 202:1223-1230.
Add to Cart SuccessfullyAdd to Cart FailedShopping cart is being updated, please waitU.S.A.
Successfully added to cart Please enter catalog numberSubmitted successfullyNetwork ErrorPlease enter your company namePlease enter your namePlease enter your emailPlease enter a valid email addressPlease enter some messageNot found.