Analytical Data
-
Gene name
RLBP1
- Application
-
Alternative Names
RLBP1;CRALBP;Retinaldehyde-binding Protein 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P12271
-
Expression Region
1-317aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEGVGT FRMVPEEEQE LRAQLEQLTT KDHGPVFGPC SQLPRHTLQK AKDELNEREE TREEAVRELQ EMVQAQAASG EELAVAVAER VQEKDSGFFL RFIRARKFNV GRAYELLRGY VNFRLQYPEL FDSLSPEAVR CTIEAGYPGV LSSRDKYGRV VMLFNIENWQ SQEITFDEIL QAYCFILEKL LENEETQING FCIIENFKGF TMQQAASLRT SDLRKMVDML QDSFPARFKA IHFIHQPWYF TTTYNVVKPF LKSKLLERVF VHGDDLSGFY QEIDENILPS DFGGTLPKYD GKAVAEQLFG PQAQAENTAF
-
Molecular Weight
39 kDa
-
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 Leucine-Zipper Protein 1) is a crucial protein involved in the visual cycle, particularly in the recycling of retinoids in the retinal pigment epithelium (RPE). Mutations in the RLBP1 gene are linked to various retinal disorders, including retinitis pigmentosa and severe visual impairments. As a result, understanding the structure and function of RLBP1 has garnered significant interest in the field of ophthalmic research and molecular biology. The recombinant expression of RLBP1 protein allows researchers to study its biochemical properties, interactions with other cellular components, and its role in retinal health and pathology. By producing RLBP1 in a controlled laboratory environment, scientists can investigate how alterations in this protein may contribute to retinal diseases and explore potential therapeutic approaches. Given that RLBP1 is involved in the transport and metabolism of vitamin A derivatives, insights from these studies could pave the way for innovative treatments aimed at restoring vision or slowing the progression of degenerative retinal conditions. Overall, the generation and analysis of RLBP1 recombinant protein are pivotal for elucidating its functions and implications in retinal physiology and disease.
