Analytical Data
-
Gene name
RLBP1
- Application
-
Alternative Names
CRALBP; Cellular retinaldehyde-binding protein
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P12271
-
Expression Region
Met1~ Phe317
-
Molecular Weight
40kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
RLBP1 (Retinal Pigment Epithelium-Bound Protein 1) is a crucial protein involved in the visual cycle and phototransduction, primarily localized in the retinal pigment epithelium (RPE). Mutations in the RLBP1 gene can lead to various retinal disorders, including retinitis pigmentosa and fundus flavimaculatus, highlighting its importance in maintaining retinal health and function. The study of RLBP1 recombinant proteins has gained significant attention as it provides valuable insights into the protein’s structural and functional properties. By expressing RLBP1 in heterologous systems, researchers aim to investigate its binding affinities, interactions with other retinal proteins, and its role in the transport of retinoids—molecules essential for vision. Furthermore, understanding the biochemical pathways involving RLBP1 may pave the way for developing therapeutic strategies for retinal diseases linked to RLBP1 dysfunction. Recombinant RLBP1 serves as a powerful tool for elucidating the mechanistic details underlying its activity and potential as a target for drug discovery in ophthalmology. The ongoing investigations into RLBP1 recombinant protein not only shed light on the basic biology of retinal function but also hold promise for innovative treatments for patients suffering from retinopathies related to this vital protein.











