Anti-Retinal S antigen抗体(ab3435)

概述

  • 产品名称
    Anti-Retinal S antigen抗体
    参阅全部 Retinal S antigen 一抗
  • 描述
    兔多克隆抗体to Retinal S antigen
  • 特异性
    Detects recombinant bovine visual Arrestin.
  • 经测试应用
    适用于: WB, IP, IHC-P, ICC/IFmore details
  • 种属反应性
    与反应: Mouse, Sheep, Cow, Human
    预测可用于: Rat, Dog, Pig
  • 免疫原

    Synthetic peptide corresponding to Rat Retinal S antigen aa 347-363.
    Sequence:

    EVATEVPFRLMHPQPED


    (Peptide available as ab4974)

性能

  • 形式
    Liquid
  • 存放说明
    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
  • 存储溶液
    Preservative: 0.05% Sodium azide
    Constituents: 0.1% BSA, 99% PBS
  • Concentration information loading...
  • 纯度
    Immunogen affinity purified
  • Primary antibody说明
    Vision involves the conversion of light into electrochemical signals that are processed by the retina and subsequently sent to, and interpreted by, the brain. The process of converting light to an electrochemical signal begins when the membrane-bound protein, rhodopsin, absorbs light within the retina. Photoexcitation of rhodopsin causes the cytoplasmic surface of the protein to become catalytically active. In the active state, rhodopsin activates transducin, a GTP binding protein. Once activated, transducin promotes the hydrolysis of cGMP by phosphodiesterase (PDE). The decrease of intracellular cGMP concentrations causes the ion channels within the outer segment of the rod or cone to close, thus causing membrane hyperpolarization and, eventually, signal transmission. Rhodopsin’s activity is believed to be shut off by its phosphorylation followed by binding of the soluble protein arrestin. Arrestins are cytosolic proteins that are involved in G protein-coupled receptor (GPCR) desensitization. Arrestin binding to activated GPCRs is phosphorylation dependent and, once bound, uncouple the GPCR from the associated heterotrimeric G proteins. There are currently 4 known mammalian isoforms, beta-Arrestin 1 (Arrestin 2), beta-Arrestin 2 (Arrestin 3), visual Arrestin (Arrestin 1), and cone arrestin. The beta- isoforms are ubiquitously expressed and are known to interact with acetylcholine and adrenergic receptors. Visual and cone Arrestins are found to interact directly with transducin.
  • 克隆
    多克隆
  • 同种型
    IgG
  • 研究领域

应用

Our Abpromise guarantee covers the use of ab3435 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

应用 Ab评论 说明
WB Use a concentration of 2 µg/ml. Can be blocked with Retinal S antigen peptide (ab4974).
IP Use at an assay dependent concentration.
IHC-P Use at an assay dependent concentration.
ICC/IF 1/100.

靶标

  • 功能
    Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase.
  • 组织特异性
    Retina and pineal gland.
  • 疾病相关
    Defects in SAG are a cause of congenital stationary night blindness Oguchi type 1 (CSNBO1) [MIM:258100]; also known as Oguchi disease. Congenital stationary night blindness is a non-progressive retinal disorder characterized by impaired night vision. CSNBO is an autosomal recessive form associated with fundus discoloration and abnormally slow dark adaptation.
  • 序列相似性
    Belongs to the arrestin family.
  • Information by UniProt
  • 数据库链接
  • 别名
    • 48 kDa protein antibody
    • Arrestin 1 antibody
    • Arrestin antibody
    • ARRS_HUMAN antibody
    • Retinal S antigen (48 KDa protein) antibody
    • Retinal S-antigen antibody
    • Rod photoreceptor arrestin antibody
    • RP47 antibody
    • S antigen antibody
    • S antigen retina and pineal gland (arrestin) antibody
    • S arrestin antibody
    • S-AG antibody
    • S-arrestin antibody
    • SAG antibody
    see all

图片

  • Western blot on recombinant bovine Retinal S antigen using ab3435.

文献

ab3435 has not yet been referenced specifically in any publications.

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