MMP-9 / ATTO 594 / S51-82
Product Details
Description | Mouse monoclonal to MMP9 (ATTO-594). MMP9, otherwise known as matrix metalloproteinase 9, is involved in the breakdown of extracellular matrix in normal physiological processes such as embryonic development, reproduction and tissue remodeling, as well as in disease processes like arthritis and metastasis. Among the family members, MMP-2, MMP-3, MMP-7 and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis (2-4). MMP activity correlates with cancer development. One mechanism of MMP regulation is transcriptional. Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein.. - | |
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Conjugate | ATTO 594 | |
Clone | S51-82 | |
Target Species | Human, Mouse, Rat | |
Applications | FC, ICC, WB, IP, IHC | |
Supplier | Biorbyt | |
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About MMP-9
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]
About ATTO 594
ATTO 594 from ATTO-Tec Gmbh has an excitation peak at 601 nm and an emission peak at 627 nm.
ATTO 594 from ATTO-Tec Gmbh has an excitation peak at 601 nm and an emission peak at 627 nm.
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