Osteopontin Rabbit Polyclonal Antibody (0806-8)

UNIPROT #

P10451

PROTEIN NAME

Osteopontin

SYNONYMS

BNSP antibody;Bone sialoprotein 1 antibody;BSP I antibody;BSPI antibody;Early T lymphocyte activation 1 antibody;ETA 1 antibody;ETA1 antibody;MGC110940 antibody;Nephropontin antibody;OPN antibody;Osteopontin antibody;osteopontin/immunoglobulin alpha 1 heavy chain constant region fusion protein antibody;OSTP_HUMAN antibody;PSEC0156 antibody;secreted phosphoprotein 1 (osteopontin, bone sialoprotein I, early T-lymphocyte activation 1) antibody;Secreted phosphoprotein 1 antibody;SPP 1 antibody;SPP-1 antibody;SPP1 antibody;SPP1/CALPHA1 fusion antibody;Urinary stone protein antibody;Uropontin antibody

SEQUENCE SIMILARITIES

Belongs to the osteopontin family.

TISSUE SPECIFICITY

Bone. Found in plasma.

POST-TRANSLATIONAL MODIFICATION

Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif.; O-glycosylated. Isoform 5 is GalNAc O-glycosylated at Thr-59 or Ser-62.

SUBCELLULAR LOCATION

Secreted.

FUNCTION

Osteopontin (OPN), also known as bone sialoprotein I (BSP-1 or BNSP), early T-lymphocyte activation (ETA-1), secreted phosphoprotein 1 (SPP1), 2ar and Rickettsia resistance (Ric),[5] is a protein that in humans is encoded by the SPP1 gene (secreted phosphoprotein 1). The murine ortholog is Spp1. Osteopontin is a SIBLING (glycoprotein) that was first identified in 1986 in osteoblasts. The prefix osteo- indicates that the protein is expressed in bone, although it is also expressed in other tissues. The suffix -pontin is derived from "pons," the Latin word for bridge, and signifies osteopontin's role as a linking protein. Osteopontin is an extracellular structural protein and therefore an organic component of bone. Synonyms for this protein include sialoprotein I and 44K BPP (bone phosphoprotein). The gene has 7 exons, spans 5 kilobases in length and in humans it is located on the long arm of chromosome 4 region 22 (4q1322.1). The protein is composed of ~300 amino acids residues and has ~30 carbohydrate residues attached, including 10 sialic acid residues, which are attached to the protein during post-translational modification in the Golgi apparatus. The protein is rich in acidic residues: 30-36% are either aspartic or glutamic acid.