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.
Theoretical MW
53 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.
Reviewed Applications
Read 1 Review rated 4 using NB100-91878 in the following applications:
Matrix metalloproteinase 3 (MMP3), also known as Stromelysin-1, SL-1, and STMY1, is a member of the matrix metalloproteinase (MMP) family. Members of the MMP family are involved in the breakdown of the extracellular matrix in response to normal physiological and disease processes; these processes include embryonic development, reproduction, tissue remodeling, arthritis and metastasis. The majority of MMP proteins are secreted into the extracellular matrix as inactive proproteins; they are activated when cleaved by an extracellular proteinase. The MMP3 gene contains four hemopexin-like domains, and is part of a cluster of MMP genes that localize to chromosome 11q22.3. This gene encodes the MMP3 enzyme that degrades fibronectin, laminin, gelatins (type I, III, IV and V), collagens (type III, IV, X, and IX), and cartilage proteoglycans. Additionally, the MMP3 enzyme activates procollagenase. Areas of interest for MMP3 include wound repair, progression of atherosclerosis, and tumor initiation.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
MMP3 - a potential target for arthritis therapies Matrix metalloproteinases (MMPs) are responsible for the degradation of extracellular matrix proteins. MMPs are essential for tissue remodeling during normal processes such as embryonic development as well as pathological conditions such as arthri... Read full blog post.
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