In the world of biochemical research and laboratory analysis, few proteins command as much attention as the Interphotoreceptor retinoid binding protein (IRBP). As someone who has sp IRBP (1-20) (human) | 298202-25-2 ent significant time reviewing literature and technical specifications regarding peptide synthesis and application, I have found the study IRBP derived peptide, R16 of this 140-kDa glycolipoprotein to be deeply fascinating.
Known scientifically as RBP3 or IRBP (RBP3), this protein is primarily secreted by photoreceptors and resides in the interphotoreceptor matrix. For those of us examining these structures, it is clear that IRBP plays a direct role in the release of all-trans retinol during the visual cycle, acting as a critical transport mechanism.
The Role of Specific Fragments in Research
The utility of IRBP in a research setting often comes down to specific fragments. When we discuss a peptide in this context, we are usually looking at highly specific sequences derived from the parent molecule. One of the most frequently cited examples in peer-reviewed journals is the human IRBP peptide 1-20.
This 20-residue sequence is a significant human IRBP peptide often used to investigate how biological systems respond to specific molecular epitopes. My experience with these materials suggests that they are indispensable tools for researchers looking to understand the complex interactions within the interphotoreceptor matrix.
Another notable variant is the IRBP derived peptide, R16, which is recognized as a biologically active fragment. Whether evaluating human IRBP peptides 1–20 or the Peptide 161-180 of human interphotoreceptor retinoid-binding prote IRBP (1-20) (human) | 298202-25-2 in (IRBP), the precision of these sequences is what makes them so valuable for high-level laboratory work.
Technical Applications and Observations
From a technical standpoint, these peptides are frequently used in antigen-specific IRBP, also known as retinol binding protein-3 (RBP-3), is a 1264 amino acid residue glycolipoprotein residing in the interphotoreceptor matrix where it is the Read more immunodetection in biological samples. This application allows for the precise tracking and verification of protein expression.
Beyond its primary transport function, some studies suggest that IRBP may have a more general role in protecting the outer retina from oxidative stress, a finding that adds layers to our understanding of why this protein is so abundant in the eye. Interestingly, it is worth noting that IRBP is also present in the pineal gland, highlighting its systemic importance beyond just ocular health.
Key Takeaways for Researchers
When sourcing or evaluating these materials, focusing on the spec by X Meng·2017·Cited by 43—Preventive effect of chrysin on experimental autoimmune uveitis triggered by injection ofhuman IRBP peptide1–20 in mice. Xiangda Meng Read more ific characteristics of the IRBP (1-20), human fragment is essential. Whether you are performing structural analysis or investigating the Interphotoreceptor retinoid binding protein (IRBP) in a controlled, non-clinical environment, keeping these details in mind ensures a higher standard of data integrity:
* Molecular Weight: Approximately 140 kDa for the full glycoprotein.
* Gene Coding: Encoded by the RBP3 gene.
* Structural Characteristics: Often described as a flexible, "cigar-shaped" molecule.
* Research Utility: Essential for mapping epitopes and understanding the visual cycle’s molecular transport.
Ultimately, the study of an IRBP-derived peptide continues to provide us with Identification of a New Epitope of Human IRBP that Induces profound insights into the complex biochemistry of the retina. By maintaining a focus on empirical data and rigorous laboratory standards, we can continue to advance our collective knowledge of these vital biological components.