antibody

anti-Secreted phosphoprotein 1 (SPP1) antibody

ABIN118005

0.2 mL

489.5 USD

polyclonal

domestic rabbit

nonconjugated

human, mouse, rat, dogs, swine

western blot, immunohistochemistry, enzyme immunoassay

anti-Secreted phosphoprotein 1 (SPP1) antibody

Rabbit

Polyclonal

Osteopontin / SPP1

Primary

0.2 mL

489.5 USD

9087961,9443783,11134063,8971479,7540371,7528752,9525990,9823334,10417195,10393964,10657301,10740253

Figure 1. Immunohistochemistry. Rabbit anti-Osteopontin was used at a 1:100-1:300 dilution to detect osteopontin by immunohistochemistry. Osteopontin is a normal component of elastic fibers in the breast (shown heavily stained in this section of human breast tumor cells). There is also weak staining of the extracellular matrix. Osteoponin is not expressed in breast tumor cells, and there is no staining of the breast cells in this section. No antigen retrieval is required.

Osteopontin (OPN) is an arginine-glycine-aspartic acid (RGD)-containing glycoprotein that interacts with integrins and CD44 as major receptors. OPN is multifunctional, with activities in cell migration, cell survival, inhibition of calcification, regulation of immune cell function, and control of tumor cell phenotype. The gene encoding OPN is called spp1. Targeting this gene has revealed that while OPN is not necessary for normal embryonic development, fertility, and health under pathogen-free conditions, loss of the protein has significant consequences in several models of injury/disease as diverse as renal injury, viral and bacterial infection, bone remodeling, and tumor growth. The fact that no other proteins seem to share a redundant activity with OPN under these conditions suggests that OPN has a unique functional role during tissue injury and stress. Interestingly, several members of the matrix metalloproteinase (MMP) family are also induced during injury/disease processes in patterns overlapping that of OPN. OPN has recently been shown to be a novel substrate for two MMPs, MMP-3 (stromelysin-1) and MMP-7 (matrilysin). There are three cleavage sites for MMP-3 in human OPN, two of which are also cleaved by MMP-7 (see cleavage diagram). Biological assays demonstrate that the MMP-cleaved OPN has increased activity in promoting both cell adhesion and migration compared with full-length OPN. In addition, inhibitory reagents were used to show that the same receptors that interact with OPN also mediate interaction of MMP-cleaved OPN with tumor cells. It is suggested that active forms of OPN at sites of tissue injury may be regulated by the activity of proteases including MMPs and that the differences in activity of modified OPN may be explained by differences in binding affinity of integrins or distinct downstream signaling events.Synonyms: BNSP, Bone Sialoprotein 1, Nephropontin, OPN, SPP-1, Secreted Phosphoprotein 1, Urinary Stone Protein, Uropontin

Synthetic peptide corresponding to Human Osteopontin conjugated to KLH using maleimide.

Dog (Canine),Human,Mouse (Murine),Pig (Porcine),Rat (Rattus)

0.02 M Potassium Phosphate, 0.12 M Sodium Chloride, pH 7.2 and 0.01 % (w/v) Sodium Azide as preservative.

75 mg/mL (by Refractometry)

Enzyme Immunoassay (EIA),Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)),Western Blotting (WB)

P10451