|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic 18 amino acid peptide from C-terminus of human MMP13.|
|Purification||Antigen affinity chromatography|
|Contains||< 0.1% sodium azide|
|Storage Conditions||Maintain refrigerated at 2-8°C for up to 1 month. For long term storage store at -20°C|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||5 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Percent identity with other species by BLAST analysis: Human, Gorilla (100%) Gibbon, Monkey, Marmoset (94%) Dog, Elephant (89%) Sheep, Bovine, Panda, Horse, Pig (83%).
All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell-matrix interactions. MMPs are Zn(2+)-binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). TIMPs have been shown to block tumor cell invasion suggesting that they act as metastasis suppressor genes.
MMP-13 was first identified in tumor cells but has since been found in synoviocytes and normal fibroblasts stimulated by IL-6 or a combination of TNF-alpha and IL-1. MMP-13 plays a significant role in cartilage collagen degradation.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.