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> Antibody > Rabbit PAb Antibody > OMD / Osteomodulin Antibody (Antigen Affinity Purified) OMD / Osteomodulin Antibody (Antigen Affinity Purified)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 50451-RP02 |
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YES |
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Mouse OMD / Osteomodulin / Osteoadherin Antibody ( Antigen Affinity Purified )
| Order or Inquire for OMD Antibody product | ![]() |
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| Detection limit is 0.5 ng/lane in WB | |||
| Detection limit is 0.00245 ng/well in ELISA |
OMD / Osteomodulin Antibody Product Information
| Immunogen : |
Recombinant mouse OMD protein ( Catalog#50451-M08H ) |
| Antibody Type : | Rabbit Polyclonal Antibody ( Antibody Purification Platform ) |
| Ig Type : |
Rabbit IgG |
| Formulation : | 0.2 μm filtered solution in PBS with 5% trehalose |
| Preparation : |
Produced in rabbits immunized with purified, human cell-derived, recombinant mouse OMD ( rM OMD ; Catalog#50451-M08H ; NP_036180.1 ; Met 1 - Ile 423 ). OMD specific IgG was purified by mouse OMD affinity chromatography |
OMD / Osteomodulin Antibody Usage Guide
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Specificity : |
Mouse OMD / Osteomodulin |
| Western blot : | This antibody can be used at 0.1 - 0.2 μg/mL with the appropriate secondary reagents to detect mouse OMD in WB. Using a DAB detection system, the detection limit for mouse OMD is approximately 2 ng/lane under non-reducing conditions and 0.5 ng/lane under reducing conditions |
| Direct ELISA : | This antibody can be used at 0.1 - 0.2 μg/mL with the appropriate secondary reagents to detect mouse OMD. The detection limit for mouse OMD is approximately 0.00245 ng/well |
| Storage : | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free. Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles. |
OMD / Osteomodulin Antibody Related Products & Topics
Related Areas:
Immunology>>Adhesion Molecule>>Extracellular Matrix Molecule>>Proteoglycan>>Osteomodulin
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Osteomodulin | Mouse | Osteomodulin/OMD Protein, Recombinant | 50451-M08H |
Antibodies:
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Mouse Osteomodulin |
WB, ELISA | Osteomodulin Antibody, Rabbit PAb | 50451-RP01 |
| Mouse Osteomodulin |
WB, ELISA | Osteomodulin Antibody, Rabbit PAb (Antigen Affinity Purified) | 50451-RP02 |
OMD / Osteomodulin Antibody Background
Mouse Osteomodulin, also known as Osteoadherin, Keratan sulfate proteoglycan osteomodulin, KSPG osteomodulin, OSAD, SLRR2C and OMD, is a secreted protein which belongs to the small leucine-rich proteoglycan (SLRP) family and Class II subfamily. SLRP family proteins are normally found in extracellular matrices, but Osteomodulin / OMD is the only member restricted to mineralized tissues. Osteomodulin / OMD is primarily expressed by osteoblasts and might have a role in regulation of mineralization. Osteomodulin / OMD was primarily present in bone trabeculae and no staining was seen in cartilage. In situ hybridization showed the strongest expression in osteoblasts close to the cartilage/bone interface of the growth plate and lower expression in diaphyseal osteoblasts. Osteomodulin / OMD is a cell binding keratan sulfate proteoglycan which was recently isolated from mineralized bovine bone and subsequently cloned and sequenced. Osteomodulin / OMD may be implicated in biomineralization processes. It has a function in binding of osteoblasts via the alpha (V) beta (3)-integrin. It is likely that Osteomodulin / OMD is an osteoblast maturation marker that is induced by osteoclast activity. Osteomodulin / OMD is also an early marker for terminally differentiated matrix producing osteoblasts.
References
- Shen,Z. et al., 1999, Matrix Biol 18 (6): 533-42.
- Clark HF. et al., 2003, Genome Res. 13:2265-70.
- Humphray S.J. et al., 2004, Nature. 429: 369-74.
- Onnerfjord P. et al., 2004, J. Biol. Chem. 279:26-33.
- Rehn, AP.et al., 2006,Biochem Biophys Res Commun.349 (3):1057-64.
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