|Application ||WB, E|
|Calculated MW||29708 Da|
|Antigen Region||96-125 aa|
|Other Names||Matrix metalloproteinase-26, MMP-26, 3424-, Endometase, Matrilysin-2, MMP26|
|Target/Specificity||This MMP26 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 96-125 amino acids from the Central region of human MMP26.|
|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||MMP26 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
|Tissue Location||Expressed specifically in uterus and placenta. Is also widely expressed in malignant tumors from different sources as well as in diverse tumor cell lines|
firstname.lastname@example.org, and receive a free "I Love Antibodies" mug.
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. The encoded protein degrades type IV collagen, fibronectin, fibrinogen, casein, vitronectin, alpha 1-antitrypsin, alpha 2-macroglobulin, and insulin-like growth factor-binding protein 1, and activates MMP9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.
de Amorim, R.F., et al. Acta Odontol. Scand. 68(4):228-231(2010)
Ban, J.Y., et al. Life Sci. 86 (19-20), 756-759 (2010) :
Deng, Y., et al. Oncol. Rep. 23(1):69-78(2010)
Johnatty, S.E., et al. PLoS Genet. 6 (7), E1001016 (2010) :
Liu, J., et al. Reprod. Biol. Endocrinol. 8, 5 (2010) :
If you have any additional inquiries please email technical services at email@example.com.