Osteopontin/SPP1 (E9Z1D) Rabbit mAb (BSA and Azide Free) #17090
- WB
- IHC
- IF
- F
Supporting Data
| REACTIVITY | M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 58-75 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- M-Mouse
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
Osteopontin/SPP1 (E9Z1D) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total osteopontin/SPP1 protein.
Species Reactivity:
Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala149 of mouse osteopontin/SPP1 protein.
Background
Osteopontin is a highly phosphorylated secreted glycoprotein expressed in a variety of cell types. Osteopontin, encoded by the gene secreted phosphoprotein 1 (SPP1), was originally isolated and cloned from a rat osteosarcoma cell line (1). Osteopontin is a highly negatively charged protein that likely regulates extracellular matrix turnover and remodeling, both in bone and other tissue (2). Osteopontin also has three highly conserved receptor-binding domains, otherwise known as arginine-glycine-aspartic acid (RGD) domains. Binding of osteopontin to cell surface integrins likely activates cell signaling pathways that regulate cell proliferation, adhesion, invasion, migration, and fibrosis (3,4). Osteopontin may be regulated by posttranslational regulation, including phosphorylation, glycosylation, and proteolytic cleavage (5). Osteopontin is also linked to several human diseases. For example, cleaved osteopontin is higher in patients suffering with cirrhosis, a disease involving fibrosis of the liver (5). Its role in the brain is unclear, but SPP1 expression in microglia, the resident macrophages of the brain, is upregulated in mouse neurodegenerative disease models, including Alzheimer’s disease (6). Osteopontin’s role in disease likely involve its function as a key mediator of inflammatory responses (4).
- Oldberg, A. et al. (1986) Proc Natl Acad Sci U S A 83, 8819-23.
- Kazanecki, C.C. et al. (2007) J Cell Biochem 102, 912-24.
- Standal, T. et al. (2004) Exp Oncol 26, 179-84.
- Lamort, A.S. et al. (2019) Cells 8, 815. doi: 10.3390/cells8080815.
- Song, Z. et al. (2021) Hepatology 73, 1594-1608.
- Sala Frigerio, C. et al. (2019) Cell Rep 27, 1293-1306.e6.
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