Anti-Osteopontin Antibody
433.5 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 992 - ER1802-15
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 100ul
Parameters
| Additional information | Synthetic peptide within mouse Osteopontin aa 100-180. |
|---|---|
| Storage and shipping | Store at +4℃ after thawing. Aliquot store at -20℃ or -80℃. Avoid repeated freeze / thaw cycles. |
0806-6
Anti-Osteopontin Antibody
Osteopontin is an extracellular matrix cell adhesion protein which is abundant in bone and synthesized by preosteoblasts, osteoblasts and osteoclastic cells that are localized in the mineralized phase of bone matrix. Osteopontin probably exists in tissue-specific isoforms that may correspond to particular cellular functions. Acts as a cytokine it involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity.
433.5 €
0806-8
Anti-Osteopontin Antibody
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.
433.5 €
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