Recombinant Human RS1 protein (GST tag N-Terminus)
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Recombinant Human RS1 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 224 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
XLRS1, RS1, Retinoschisin, X-linked juvenile retinoschisis protein
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human RS1 protein (GST tag N-Terminus) (AB159464)
ab159464 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
RS1 is involved in maintaining the structural organization of the retinal layers. It participates in forming a protein complex that helps maintain the extracellular space and regulates cellular adhesion within the retina contributing to the integrity and stability of retinal architecture. The structure of the retina is important for proper signal transduction related to visual processing. The RS1 protein acts as a stabilizing factor reducing retinal detachment and disruptions that can impact vision clarity and focus.
Pathways
Retinoschisin interacts with cellular adhesion pathways and signal transduction within retinal cells. This protein appears to influence the Wnt signaling pathway which plays a role in cell-to-cell communication in the retina. Additionally RS1 associates with the neuropilin protein family which includes proteins involved in axon guidance and vascular patterning therefore influencing the development and maintenance of the retinal structure. These pathways highlight the potential impact of RS1 on visual processing and retinal health.
Specifications
Form
Liquid
General info
Function
Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells (PubMed : 27114531). Required for normal structure and function of the retina (PubMed : 19093009).
Target data
Product promise
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