货号 | AF942-SP |
别名 | Basement-membrane protein 40; BM-40; ONcysteine-rich protein; Osteonectin; Secreted protein acidic and rich in cysteine; secreted protein, acidic, cysteine-rich (osteonectin) | 全称 | Secreted Protein Acidic and Rich in Cysteine |
反应种属 | Mouse |
应用 | Western Blot(0.1 µg/mL) Immunohistochemistry(5-15 µg/mL) Intracellular Staining by Flow Cytometry(2.5 µg/106cells) |
目标/特异性 | Detects mouse SPARC in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 1% cross-reactivity with recombinant human SPARC is observed. |
使用方法 | Western Blot: 0.2 µg/mL Immunohistochemistry: 1-15 µg/mL Intracellular Staining by Flow Cytometry: 0.25 µg/106cells |
来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 6678 (Human); 20692 (Mouse) |
应用文献 | |
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. CSF1-ETS2-induced microRNA in myeloid cells promote metastatic tumor growth. | |
纯化方式 | Antigen Affinity-purified |
免疫原 | Mouse myeloma cell line NS0-derived recombinant mouse SPARC/Osteonectin Ala18-Ile302 Accession # P07214 |
生物活性 | Mouse |
标记 | Unconjugated |
溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
背景 | SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40 (1-5). It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 302 amino acid (aa), 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs (1-5). Crystal structure shows that residues implicated in cell binding, inhibition of cell spreading and disassembly of focal adhesions cluster on one face of SPARC, while a collagen binding epitope and an N-glycosylation site are opposite this face (6). SPARC is produced by fibroblasts, capillary endothelial cells, platelets, and macrophages, especially in areas of tissue morphogenesis and remodeling (3, 7). SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation (3-5). For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF (3-5). SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis (5, 8). SPARC is potentially cleaved by metalloproteinases, producing an angiogenic peptide that includes the copper-binding sequence KGHK (7). Paradoxically, SPARC is highly expressed in many tumor types, yet expression mainly decreases the likelihood of metastasis and confers sensitivity to chemotherapy and radiation (4, 9, 10). Stabilin-1, which is expressed on alternately activated macrophages, is the first SPARC receptor to be identified. It binds the SPARC EC domain and mediates endocytosis for degradation (11). Mature mouse SPARC shows 97%, 92%, 92%, 92%, and 83% aa identity with rat, human, dog, cow, and chick SPARC, respectively. |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
|
SPARC/Osteonectin in Mouse Embryo. SPARC/Osteonectin was detected in immersion fixed frozen sections of mouse embryo (E15) using Mouse SPARC/Osteonectin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF942) at 1.7 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to developing cartilage. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections. |