Anti-Osteopontin (SPP1), human C-Terminus [LF-166] Antibody

This rabbit IgG polyclonal antibody was generated against recombinant protein E. coli and recognizes human, cow, and sheep Osteopontin (SPP1).

Highlights:

  • Recognizes human, cow, and sheep SPP1- Epitope Carboxy-terminal domain after cleavage by thrombin
  • Suitable for Immunohistochemistry and Western Blot applications

Osteopontin is a phosphoglycoprotein synthesized in a variety of tissues and cells. It was originally identified as a bone matrix protein and subsequently as a cytokine produced by various immune and transformed cell lines. OPN is a biomarker for various types of cancers and inflammatory diseases. Excessive or dysregulated OPN expression has been linked to the pathogenesis of both autoimmune disorders such as multiple sclerosis, systemic lupus erythematosus, rheumatoid arthritis, atherosclerosis and other inflammatory diseases including cardiovascular disease, chronic obstructive pulmonary disease, inflammatory bowel disease, liver disease and asthma.

From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
ENH093-FP
Anti-Osteopontin (SPP1), human C-Terminus [LF-166] Antibody
100uL In stock
Regular Price:$306.00
On Sale:

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Specifications

Product Type: Antibody
Accession ID: P10451.1
Antigen: Osteopontin (SPP1), human
Molecular Weight: 35148 Da
Clonality: Polyclonal
Clone Name: LF-166
Reactivity: Human, cow, sheep
Immunogen: Recombinant E. coli
Species Immunized: Rabbit
Epitope: Carboxy-terminal domain after cleavage by thrombin
Buffer: Whole serum
Tested Applications: WB 1:1000, IHC 1:300
Storage: -80C
Shipped: Dry Ice

Provider
From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research.
References
  1. Golledge J, McCann M, Mangan S, Lam A, Karan M. Osteoprotegerin and osteopontin are expressed at high concentrations within symptomatic carotid atherosclerosis. Stroke. 2004 Jul;35(7):1636-41.
  2. Connolly JM, Alferiev I, Clark-Gruel JN, Eidelman N, Sacks M, Palmatory E, Kronsteiner A, Defelice S, Xu J, Ohri R, Narula N, Vyavahare N, Levy RJ.Triglycidylamine crosslinking of porcine aortic valve cusps or bovine pericardium results in improved biocompatibility, biomechanics, and calcification resistance: chemical and biological mechanisms. Am J Pathol. 2005 Jan;166(1):1-13.
  3. Fassina L, Saino E, De Angelis MG, Magenes G, Benazzo F, Visai L. Low-power ultrasounds as a tool to culture human osteoblasts inside cancellous hydroxyapatite. Bioinorg Chem Appl. 2010:456240.
  4. Orsini G, Majorana A, Mazzoni A, Putignano A, Falconi M, Polimeni A, Breschi L. Immunocytochemical detection of dentin matrix proteins in primary teeth from patients with dentinogenesis imperfecta associated with osteogenesis imperfecta. Eur J Histochem. 2014 Dec 1;58(4):2405.
  5. von Marschall Z, Mok S, Phillips MD, McKnight DA, Fisher LW. Rough endoplasmic reticulum trafficking errors by different classes of mutant dentin sialophosphoprotein (DSPP) cause dominant negative effects in both dentinogenesis imperfecta and dentin dysplasia by entrapping normal DSPP. J Bone Miner Res. 2012 Jun;27(6):1309-21.
  6. Qi L, Basset C, Averseng O, Quéméneur E, Hagège A, Vidaud C.Characterization of UO2(2+) binding to osteopontin, a highly phosphorylated protein: insights into potential mechanisms of uranyl accumulation in bones. Metallomics. 2014 Jan;6(1):166-76.

If you publish research with this product, please let us know so we can cite your paper.

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