OPN Polyclonal Antibody (AN005950L)
For research use only.
| Verified Samples |
Verified Samples in WB: Rat kidney Verified Samples in IHC: Human kidney, Human liver |
| Dilution | WB 1:1000-1:2000, IHC 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Rat |
| Applications | WB, IHC |
| Clonality | Polyclonal |
| Immunogen | Recombinant Mouse OPN protein expressed by Mammalian |
| Abbre | Osteopontin/OPN |
| Synonyms | BSP, Eta, Secreted Phosphoprotein, Early T-Lymphocyte Activation, BNSP, Bone Sialoprotein I, BSP1, Early T-Lymphocyte Activation 1, Secreted Phosphoprotein 1, Eta-1, Op, Spp-1, Spp1 |
| Swissprot | |
| Calculated MW | 35 kDa |
| Observed MW |
60 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Secreted |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
| background | Osteopontin (OPN, previously also referred to as transformation-associated secreted phosphoprotein, bone sialoprotein I, 2ar, 2B7, early T lymphocyte activation 1 protein, minopotin, calcium oxalate crystal growth inhibitor protein), is a secreted, highly acidic, calcium-binding, RGD-containing, phosphorylated glycoprotein originally isolated from bone matrix. Subsequently, OPN has been found in kidney, placenta, blood vessels and various tumor tissues. Many cell types (including macrophages, osteoclasts, activated T cells, fibroblasts, epithelial cells, vascular smooth muscle cells, and natural killer cells) can express OPN in response to activation by cytokines, growth factors or inflammatory mediators. Elevated expression of OPN has also been associated with numerous pathobiological conditions such as atherosclerotic plaques, renal tubulointerstitial fibrosis, granuloma formations in tuberculosis and silicosis, neointimal formation associated with balloon catheterization, metastasizing tumors, and cerebral ischemia. Mouse OPN cDNA encodes a 294 amino acid (aa) residue precursor protein with a 16 aa residue predicted signal peptide that is cleaved to yield a 278 aa residue mature protein with an integrin binding sequence (RGD), and N- and O-glycosylation sites. OPN has been shown to bind to different cell types through RGD-mediated interaction with the integrins alpha v beta 1, alpha v beta 3, alpha v beta 5, and non-RGD-mediated interaction with CD44 and the integrins alpha 8 beta 1 or alpha 9 beta 1. Functionally, OPN is chemotactic for macrophages, smooth muscle cells, endothelial cells and glial cells. OPN has also been shown to inhibit nitric oxide production and cytotoxicity by activated macrophages. Human, mouse, rat, pig and bovine OPN share from approximately 40-80% amino acid sequence identity. Osteopontin is a substrate for proteolytic cleavage by thrombin, enterokinase, MMP-3 and MMP-7. The functions of OPN in a variety of cell types were shown to be modified as a result of proteolytic cleavage. |
Other Clones
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Unconjugated
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