|Application ||WB, E|
|Calculated MW||53412 Da|
|Antigen Region||56-84 aa|
|Other Names||Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase, PMNL-CL, MMP8, CLG1|
|Target/Specificity||This MMP8 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 56-84 amino acids from the N-terminal region of human MMP8.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP8 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Can degrade fibrillar type I, II, and III collagens.|
|Cellular Location||Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules|
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Provided below are standard protocols that you may find useful for product applications.
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. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
Li, Y., et al. J. Surg. Res. 163 (2), E99-E104 (2010) :
Romero, R., et al. Am. J. Obstet. Gynecol. 203 (4), 361 (2010) :
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Alexander, J.S., et al. Mult. Scler. 16(7):801-809(2010)
Djuric, T., et al. J. Clin. Lab. Anal. 24(4):246-251(2010)
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