Rockland Immunochemicals, Inc.'s Osteopontin Antibody is a Rabbit Polyclonal antibody. This antibody has been shown to work in applications such as: EIA, Immunoassay, ELISA, Immunohistochemistry, Immunoprecipitation, and Western Blot. The Osteopontin Antibody was generated using Spp1 as the antigen and it reacts with Homo Sapiens, and Human.
Description
Anti-Osteopontin Antibody recognizes Osteopontin (OPN) which is an arginine-glycine-aspartic acid (RGD)-containing glycoprotein that interacts with integrins and CD44 as major receptors. OPN is multifunctional, with activities in cell migration, cell survival, inhibition of calcification, regulation of immune cell function, and control of tumor cell phenotype. The gene encoding OPN is called spp1. Targeting this gene has revealed that while OPN is not necessary for normal embryonic development, fertility, and health under pathogen-free conditions, loss of the protein has significant consequences in several models of injury/disease as diverse as renal injury, viral, and bacterial infection, bone remodeling, and tumor growth. The fact that no other proteins seem to share a redundant activity with OPN under these conditions suggests that OPN has a unique functional role during tissue injury and stress. Interestingly, several members of the matrix metalloproteinase (MMP) family are also induced during injury/disease processes in patterns overlapping that of OPN. OPN has recently been shown to be a novel substrate for two MMPs, MMP-3 (stromelysin-1) and MMP-7 (matrilysin). There are three cleavage sites for MMP-3 in human OPN, two of which are also cleaved by MMP-7 (see cleavage diagram). Biological assays demonstrate that the MMP-cleaved OPN has increased activity in promoting both cell adhesion and migration compared with full-length OPN. In addition, inhibitory reagents were used to show that the same receptors that interact with OPN also mediate interaction of MMP-cleaved OPN with tumor cells. It is suggested that active forms of OPN at sites of tissue injury may be regulated by the activity of proteases including MMPs and that the differences in activity of modified OPN may be explained by differences in binding affinity of integrins or distinct downstream signaling events. Osteopontin can be responsible for diseases such as lung and prostate cancers, nephrolithiasis, hepatocellular carcinoma, osteoporosis and arteriosclerosis. Anti-Osteopontin is useful for researchers interested in Stem Cell and Extracellular Matrix Antibodies