Thermo Fisher Scientific OPN-R Recombinant Rabbit Monoclonal Antibody (24H5L3)
Recombinant rabbit monoclonal antibody recognizing human and mouse OPN-R. Validated for WB and ICC/IF. Offers high specificity, lot-to-lot consistency, and animal-free formulation. Suitable for research on osteopontin-related signaling and disease mech...
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Applications
| Application | Tested Dilution | Publications |
|---|---|---|
| Western Blot (WB) | 1–2 µg/mL | View 1 publication |
| Immunocytochemistry (ICC/IF) | 2 µg/mL | – |
Product Specifications
| Category | Details |
|---|---|
| Species Reactivity | Human, Mouse |
| Published Species | Human |
| Host / Isotype | Rabbit / IgG |
| Expression System | Expi293 |
| Class | Recombinant Monoclonal |
| Type | Antibody |
| Clone | 24H5L3 |
| Immunogen | Peptide corresponding to Human SPP1 (aa 158–165) |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 0.5 mg/mL |
| Purification | Protein A |
| Storage Buffer | PBS, pH 7.2 |
| Contains | 0.09% sodium azide |
| Storage Conditions | Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles. |
| Shipping Conditions | Wet ice |
| RRID | AB_2633064 |
Product Specific Information
This antibody is predicted to react with Monkey, Rabbit, and Bat.
Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The antibody DNA sequences from immunoreactive rabbits are cloned, and individual clones are screened to select optimal candidates for production.
Advantages:
- Improved specificity and sensitivity
- Lot-to-lot consistency
- Animal origin-free formulation
- Broader immunoreactivity due to the rabbit immune repertoire
Target Information
Osteopontin (OPN) is a 34 kDa extracellular matrix protein with a cell-binding domain. Initially identified as a major component of the non-collagenous bone matrix, OPN is now known to be present in many adult tissues and body fluids.
Functions and Roles:
- Involved in bone mineralization, cell adhesion, and migration
- Plays roles in chronic inflammation and cellular transformation
- Proteolytic cleavage by thrombin and matrix metalloproteinases modulates integrin-binding properties
- Thrombin-cleaved fragments are overexpressed in malignant glial tumors, providing survival advantages and novel substrates for proteases such as plasmin and cathepsin D
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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