GRK1抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P10933(GRK1 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P10933(GRK1 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

GRK1 (G protein-coupled receptor kinase 1), also known as rhodopsin kinase, is a serine/threonine kinase primarily expressed in retinal photoreceptor cells. It plays a critical role in regulating the activity of G protein-coupled receptors (GPCRs), particularly rhodopsin, the light-sensitive receptor in rod cells. Following light activation, GRK1 phosphorylates the cytoplasmic tail of rhodopsin, initiating its desensitization by promoting arrestin binding. This process is essential for terminating phototransduction signals and enabling photoreceptor recovery, ensuring proper visual function. Structurally, GRK1 contains a conserved kinase domain and a regulator of G protein signaling (RGS) domain, which facilitates interactions with activated G proteins.

Antibodies targeting GRK1 are vital tools for studying retinal biology and GPCR signaling mechanisms. They are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to detect GRK1 expression, localization, and post-translational modifications in retinal tissues or cell models. Dysregulation of GRK1 has been linked to retinal disorders such as Oguchi disease, a congenital stationary night blindness caused by GRK1 mutations. Research using GRK1 antibodies also explores its interaction with other proteins, such as recoverin, which modulates its kinase activity in a calcium-dependent manner. These studies contribute to understanding vision-related pathologies and potential therapeutic strategies, including gene therapy for inherited retinal diseases. Commercial GRK1 antibodies are typically raised in rabbits or mice, with validation in knockout controls to ensure specificity.