Osteopontin Antibody [K22J24] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:2000

Application
WB, IP, IHC

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
35 kDa 45 kDa, 60-65 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Osteopontin Antibody [K22J24] detects endogenous levels of total Osteopontin protein.

Clone
K22J24

Synonym(s)
BNSP, OPN, PSEC0156, SPP1, Osteopontin, Bone sialoprotein 1, Nephropontin, Secreted phosphoprotein 1, Urinary stone protein, Uropontin, SPP-1

Background
Osteopontin, also termed OPN or secreted phosphoprotein 1 (SPP1), is a secreted, highly phosphorylated, acidic glycophosphoprotein of the SIBLING family that localizes to mineralized extracellular matrices and body fluids and functions as a matricellular regulator at the interface of structural matrix and cell signaling in bone and immune tissues. The protein contains an Arg‑Gly‑Asp (RGD) integrin‑binding motif, poly‑aspartate segments that interact with hydroxyapatite, multiple phosphorylation and glycosylation sites, and CD44‑binding sequences; these elements allow osteopontin to bind αvβ3 and other integrins, CD44 isoforms, and mineral surfaces, and to bridge cells to the extracellular matrix while modulating intracellular signaling. In bone, osteopontin is enriched at cement lines and resorption surfaces, where its RGD motif engages αvβ3 integrin on osteoclasts to support adhesion, actin ring organization, and resorptive activity, while its acidic, calcium‑binding regions interact with hydroxyapatite and contribute to regulation of crystal growth and mineralization, helping define the mechanical properties and remodeling capacity of articular and trabecular bone. As an immunomodulatory cytokine‑like factor, osteopontin is produced by activated T cells, macrophages, dendritic cells, and stromal cells and influences Th1/Th17‑type responses by promoting macrophage and T‑cell recruitment, enhancing survival, and regulating production of IL‑12, IL‑10, IFN‑γ, and other inflammatory mediators, thereby shaping chronic inflammatory environments in tissues such as joints, vessels, and the central nervous system. Osteopontin signals through integrins and CD44 to activate intracellular pathways including PI3K–Akt and NF‑κB; engagement of these receptors leads to Akt phosphorylation, IKK activation, IκBα degradation, NF‑κB nuclear translocation, and up‑regulation of urokinase‑type plasminogen activator and matrix metalloproteinase‑linked programs that increase cell motility, invasion, and survival in cancer models. Secreted osteopontin in breast cancer xenografts regulates a network of genes in VEGF, PDGF, IL‑10, GM‑CSF, apoptosis, and proliferation pathways, consistent with a role in controlling angiogenesis, immune modulation, and local tumor progression through receptor‑mediated signaling rather than purely structural matrix functions. In bone metabolism and bone diseases, osteopontin expression correlates with remodeling activity, fracture repair, and orthodontic tooth movement, and osteopontin‑rich matrices show altered resorption and mineralization characteristics in osteoporosis and osteoarthritis. High osteopontin levels are detected in atherosclerotic plaques, rheumatoid joints, and various tumors, and its combined integrin/CD44 binding, mineral affinity, and cytokine‑like signaling properties link it to vascular calcification, chronic synovitis, fibrosis, and metastatic niches.

Background

Osteopontin, also termed OPN or secreted phosphoprotein 1 (SPP1), is a secreted, highly phosphorylated, acidic glycophosphoprotein of the SIBLING family that localizes to mineralized extracellular matrices and body fluids and functions as a matricellular regulator at the interface of structural matrix and cell signaling in bone and immune tissues. The protein contains an Arg‑Gly‑Asp (RGD) integrin‑binding motif, poly‑aspartate segments that interact with hydroxyapatite, multiple phosphorylation and glycosylation sites, and CD44‑binding sequences; these elements allow osteopontin to bind αvβ3 and other integrins, CD44 isoforms, and mineral surfaces, and to bridge cells to the extracellular matrix while modulating intracellular signaling. In bone, osteopontin is enriched at cement lines and resorption surfaces, where its RGD motif engages αvβ3 integrin on osteoclasts to support adhesion, actin ring organization, and resorptive activity, while its acidic, calcium‑binding regions interact with hydroxyapatite and contribute to regulation of crystal growth and mineralization, helping define the mechanical properties and remodeling capacity of articular and trabecular bone. As an immunomodulatory cytokine‑like factor, osteopontin is produced by activated T cells, macrophages, dendritic cells, and stromal cells and influences Th1/Th17‑type responses by promoting macrophage and T‑cell recruitment, enhancing survival, and regulating production of IL‑12, IL‑10, IFN‑γ, and other inflammatory mediators, thereby shaping chronic inflammatory environments in tissues such as joints, vessels, and the central nervous system. Osteopontin signals through integrins and CD44 to activate intracellular pathways including PI3K–Akt and NF‑κB; engagement of these receptors leads to Akt phosphorylation, IKK activation, IκBα degradation, NF‑κB nuclear translocation, and up‑regulation of urokinase‑type plasminogen activator and matrix metalloproteinase‑linked programs that increase cell motility, invasion, and survival in cancer models. Secreted osteopontin in breast cancer xenografts regulates a network of genes in VEGF, PDGF, IL‑10, GM‑CSF, apoptosis, and proliferation pathways, consistent with a role in controlling angiogenesis, immune modulation, and local tumor progression through receptor‑mediated signaling rather than purely structural matrix functions. In bone metabolism and bone diseases, osteopontin expression correlates with remodeling activity, fracture repair, and orthodontic tooth movement, and osteopontin‑rich matrices show altered resorption and mineralization characteristics in osteoporosis and osteoarthritis. High osteopontin levels are detected in atherosclerotic plaques, rheumatoid joints, and various tumors, and its combined integrin/CD44 binding, mineral affinity, and cytokine‑like signaling properties link it to vascular calcification, chronic synovitis, fibrosis, and metastatic niches.

References
https://pubmed.ncbi.nlm.nih.gov/31996665/ https://pubmed.ncbi.nlm.nih.gov/19798593/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%