在线日韩日本国产亚洲丨少妇伦子伦情品无吗丨欧美性猛交xxxx免费看蜜桃丨精品人妻系列无码一区二区三区丨亚洲精品无码不卡在线播放

Your Good Partner in Biology Research

OSBP Antibody

  • 中文名稱:
    OSBP兔多克隆抗體
  • 貨號:
    CSB-PA017243GA01HU
  • 規格:
    ¥3,900
  • 其他:

產品詳情

  • Uniprot No.:
  • 基因名:
    OSBP
  • 別名:
    OSBP 1 antibody; OSBP antibody; OSBP1_HUMAN antibody; Oxysterol binding protein 1 antibody; Oxysterol-binding protein 1 antibody
  • 宿主:
    Rabbit
  • 反應種屬:
    Human,Mouse,Rat
  • 免疫原:
    Human OSBP
  • 免疫原種屬:
    Homo sapiens (Human)
  • 抗體亞型:
    IgG
  • 純化方式:
    Antigen Affinity Purified
  • 濃度:
    It differs from different batches. Please contact us to confirm it.
  • 保存緩沖液:
    PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
  • 產品提供形式:
    Liquid
  • 應用范圍:
    ELISA,WB,IHC,IP
  • Protocols:
  • 儲存條件:
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 貨期:
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
  • 用途:
    For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產品評價

靶點詳情

  • 功能:
    Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability.
  • 基因功能參考文獻:
    1. the component proteins of the machinery, OSBP, VAP, SAC1, and PITPNB, are all essential host factors for AiV replication. Importantly, the machinery is directly recruited to the RNA replication sites through previously unknown interactions of VAP/OSBP/SAC1 with the AiV proteins and with ACBD3. PMID: 29367253
    2. results demonstrate that Sac1 expression in either the ER or Golgi apparatus has a minimal impact on the PI-4P that regulates OSBP activity or recruitment to contact sites PMID: 28471037
    3. Cholesterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP have been described. PMID: 28978670
    4. Data suggest that OSBP shifts the distribution of phosphatidylinositol 4-phosphate upon localization to endoplasmic reticulum-Golgi contact sites. PMID: 26601944
    5. Our results identify OspB as a regulator of mTORC1 and mTORC1-dependent cell proliferation early during S. flexneri infection and establish a role for IQGAP1 in mTORC1 signaling PMID: 26473364
    6. These results suggest that poliovirus proteins modulate PI4KB activity and provide PI4P for recruitment of OSBP to accumulate unesterified cholesterol on virus-induced membrane structure for formation of a virus replication complex. PMID: 24527995
    7. OSBP-mediated back transfer of phosphatidylinositol 4-phosphate might coordinate the transfer of other lipid species at the endoplasmic reticulum-Golgi interface. PMID: 24209621
    8. OSBP is required for efficient replication of intracellular S. Typhimurium. PMID: 21988961
    9. Data indicate that phosphorylation on two serine-rich motifs, S381-S391 (site 1) and S192, S195, S200 (site 2), specifically controls oxysterol-binding protein (OSBP) activity at the endoplasmic reticulum (ER). PMID: 22875984
    10. PKD negatively regulates HCV secretion/release by attenuating OSBP and CERT functions by phosphorylation inhibition. This study identifies the key role of the Golgi components in the HCV maturation process. PMID: 21285358
    11. Results identify a novel substrate of protein kinase D at the Golgi, the oxysterol-binding protein OSBP. PMID: 20444975
    12. This review summarizes recent evidence of sterol transfer activity by OSBP, suggesting seemingly disparate functions that could be the result of alterations in membrane sterol distribution or ancillary to this primary activity. PMID: 20545625
    13. Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. PMID: 20178991
    14. OSBP was found to function as a cholesterol-binding scaffolding protein coordinating the activity of two phosphatases to control the extracellular signal-regulated kinase (ERK) signaling pathway PMID: 15746430
    15. Regulation of ceramide transport protein by OSBP, sterols, and vesicle-associated protein reveals a novel mechanism for integrating sterol regulatory signals with ceramide transport and phingomyelin synthesis in the Golgi apparatus. PMID: 16571669
    16. OSBP is able to sense both membrane cholesterol and oxidized sterols and link this information to the ERK1/2 signaling pathway. PMID: 18165705
    17. functional role of OSBP in the HCV maturation process. PMID: 19570870

    顯示更多

    收起更多

  • 亞細胞定位:
    Cytoplasm, cytosol. Cytoplasm, perinuclear region. Golgi apparatus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network.
  • 蛋白家族:
    OSBP family
  • 組織特異性:
    Widely expressed.
  • 數據庫鏈接:

    HGNC: 8503

    OMIM: 167040

    KEGG: hsa:5007

    STRING: 9606.ENSP00000263847

    UniGene: Hs.597091



主站蜘蛛池模板: 三级做爰高清视频| 国产亚洲精品精华液| 国产高清在线精品一区| 两个人看的www在线观看| 亚洲有无码av在线播放| 韩国午夜福利片在线观看| 国产在线无码一区二区三区| 日日碰狠狠添天天爽超碰97| 久久久久久无码av成人影院| 亚洲成a∨人片在线观看不卡 | 亚洲成在人线av| 中文字幕人妻被公上司喝醉在线| 国产福利萌白酱精品一区| 日韩欧美mv在线观看免费| 无码免费一区二区三区| 国产激情久久久久久熟女老人av| av在线亚洲男人的天堂| 亚州中文字幕无码中文字幕| 国产亚洲精品一区在线播放| av天堂亚洲区无码先锋影音 | 亚洲妇女行蜜桃av网网站| 国产精品久久久久9999不卡| 国产aⅴ夜夜欢一区二区三区| 亚洲欧美日韩精品久久| 少妇被黑人到高潮喷出白浆| 色欲天天婬色婬香综合网完整版 | 国产成人av在线播放影院| 麻花豆传媒剧国产免费mv观看| 久久精品国产久精国产| 欧美日韩欧美| 毛茸茸厕所偷窥xxxx| 曰的好深好爽免费视频网站| 国产在线精品一区二区三区| 鲁鲁鲁爽爽爽在线视频观看| 成人综合婷婷国产精品久久 | 亚洲色精品三区二区一区| 国产午夜视频在线观看| 无码人妻品一区二区三区精99| 天堂8а√中文在线官网 | 亚洲熟妇无码av不卡在线观看| 小草社区视频在线观看|