Recombinant Human Rhodopsin (RHO) Protein (His-SUMO)

Name: Recombinant Human Rhodopsin (RHO) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09431P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Rhodopsin (RHO) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P08100
Target Symbol	RHO
Synonyms	CSNBAD1; MGC138309; MGC138311; OPN 2; OPN2; opsd; OPSD_HUMAN; opsin 2; Opsin 2 rod pigment; Opsin-2; Opsin2; Retinitis Pigmentosa 4; Retinitis pigmentosa 4 autosomal dominant; RHO; Rhodopsin; RP 4; RP4
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
Expression Range	1-36aa
Protein Length	Partial
Mol. Weight	20.2kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth. Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling.
Subcellular Location	Membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment.
Protein Families	G-protein coupled receptor 1 family, Opsin subfamily
Database References	HGNC: 10012 OMIM: 180380 KEGG: hsa:6010 STRING: 9606.ENSP00000296271 UniGene: Hs.247565
Associated Diseases	Retinitis pigmentosa 4 (RP4); Night blindness, congenital stationary, autosomal dominant 1 (CSNBAD1)
Tissue Specificity	Rod shaped photoreceptor cells which mediate vision in dim light.

Gene Functions References

using cryo-electron microscopy, it is shown that the major interactions between activated rhodopsin and Gi are mediated by the C-terminal helix of the Gi alpha-subunit, which is wedged into the cytoplasmic cavity of the transmembrane helix bundle and directly contacts the amino terminus of helix 8 of rhodopsin PMID: 29899450
The identification of the pathogenic variant p.E113 K is the first description of a naturally-occurring mutation in the Schiff base counterion of RHO in patients. The heterozygous mutation c.337G > A in exon 1 was confirmed in the retinitis pigmentosa index patient as well as in five stationary night blindness-affected relatives. PMID: 27812022
data provide the first evidence that T17M rhodopsin mutant disrupts C3 secretion via the induction of ROS and the suppression of TWIST1. PMID: 28569420
Wild-type opsin mainly formed oligomers. Only a minor population formed aggregates. The G188R opsin mutant mainly formed aggregates. When wild-type opsin and G188R opsin were coexpressed in cells, properly folded wild-type opsin did not aggregate with G188R opsin and was trafficked normally to the cell membrane. The autosomal dominant phenotype due to misfolded opsin mutants is not due to WT-mutant physical interaction. PMID: 27117643
Data suggest that retinitis pigmentosa-associated mutation G51A behaves differently in human rhodopsin compared to bovine rhodopsin; human rhodopsin is more thermally stable than ancestral ancestrally reconstructed mammalian rhodopsin. PMID: 28369862
These findings provide a new understanding of the effects of oxLDL on endothelial proliferation, which is essential for developing new treatments against neovascularization and progression of atherosclerosis. PMID: 28701359
Study reports an X-ray free electron laser crystal structure of the rhodopsin-arrestin complex, in which the phosphorylated C terminus of rhodopsin forms an extended intermolecular beta sheet with the N-terminal beta strands of arrestin. Phosphorylation was detected at rhodopsin C-terminal tail residues T336 and S338. PMID: 28753425
results suggest that nonsense-mediated mRNA decay modulates the severity of retinitis pigmentosa in patients with nonsense mutations in the rhodopsin gene PMID: 26416182
both the charged G90D(2.57) and the hydrophobic T94I(2.61) mutation alter the dark state by weakening the interaction between the Schiff base (SB) and its counterion E113(3.28) We propose that this interference with the tight regulation of the dim light photoreceptor rhodopsin increases background noise in the visual system and causes the loss of night vision characteristic for CSNB patients. PMID: 27458239
A mutation-independent strategy appears viable in this specific context but certain mutations could significantly influence ribozyme or RNAi efficacy through impact on accessibility at the target annealing site/region. PMID: 28715844
a recurrent missense mutation (c.403C > T, p.R135W) in the rhodopsin (RHO) gene cosegregated with all retinitis pigmentosa affected individuals in the family. PMID: 26794436
Autosomal recessive retinitis pigmentosa with homozygous rhodopsin mutation E150K and non-coding cis-regulatory variants in CRX-binding regions of SAMD7. PMID: 26887858
Functional role of positively selected amino acid substitutions in mammalian rhodopsin evolution has been uncovered for a large number of mammalian species. PMID: 26865329
Our study shows that RHO mutations are a major cause of adRP in this cohort and are responsible for 28% of adRP families. PMID: 26962691
analysis of the crystal structure of the rhodopsin-arrestin complex PMID: 26467309
A whole-exome sequencing approach led to identification of a deletion in RHO through detection of a new linked variant in COL6A6 in autosomal dominant retinitis pigmentosa. PMID: 26321861
These insights into the dynamics of the ground states and the early photocycle stages enhance our understanding of the channel function of Channel rhodopsin. PMID: 26114863
Studies indicate that misfolding of rhodopsin can result in disruptions in cellular protein homeostasis, or proteostasis. PMID: 26427449
FIP3 (RAB11-FIP3) promotes the activity of Rab11a and the ASAP1 in the Arf4-dependent ciliary transport of the sensory receptor rhodopsin. PMID: 25673879
RHO polymorphisms (rs7984, rs2855557 and rs2410) and haplotypes may confer remarkable susceptibility to age-related macular degeneration PMID: 26045836
The study identified a RHO gene mutation (p.Thr58Met) not previously reported in RP in a patient with sector retinitis pigmentosa (RP). PMID: 25265376
Similar vacuolization in photoreceptor outer segment discs of transgenic mice expressing human rhodopsin with a T17M mutation or non-glycosylated form of rhodopsin was found. Non-glycosylated rhodopsin is unstable and is regulated via ubiquitin pathway PMID: 25637522
reveal the spectrum and frequency of RHO mutations in Chinese patients with different forms of retinitis pigmentosa and demonstrate that RHO mutations account for a high proportion of autosomal dominant retinitis pigmentosa cases PMID: 25221422
show that although the basic activation pathways of human and bovine rhodopsin are similar, structural deviations exist in the inactive conformation and during receptor activation, even between closely related rhodopsins PMID: 26105054
Rer1p regulates the ER retention of immature or misfolded rhodopsin and modulates its intracellular trafficking through the early secretory pathway. PMID: 25096327
crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin, determined by serial femtosecond X-ray laser crystallography PMID: 26200343
RHO has an intrinsic water pathway, which in the receptors' resting state is interrupted by a hydrophobic layer of amino acid residues and upon agonist binding, opened to a continuous intrinsic water channel. PMID: 25203160
ERdj5 is a member of the proteostasis network that regulates rod opsin biogenesis and supports a role for disulfide bond formation/reduction in rod opsin biogenesis and disease. PMID: 25055872
This retrospective study provides a wide spectrum of mutations in the RHO gene in Spanish patients with autosomal dominant Retinitis Pigmentosa . PMID: 25408095
Data indicate that transfected human channelrhodopsin-2 (rhodopsin) increased the action potential in the rat spinal cord and activated the calcium channel in dorsal root ganglion neurons. PMID: 25171072
In this report we describe a New Zealand family, of European heritage, affected by a sectoral type RP phenotype in association with a novel rhodopsin mutation (proline-170-histidine) in a highly conserved site. PMID: 24918165
Data indicate that the number of nanodomains present in a single disc was dependent on the number of rhodopsin molecules incorporated into the membrane. PMID: 25305340
Electron paramagnetic resonance spectra of the spin-labeled samples indicate that the extracellular residues of RHO retain more rigidity in the denatured states than the cytoplasmic residues. PMID: 25268658
tHE results OF THIS STUDY identify a novel pathogenic mechanism in which the glycosylation-deficient rhodopsins are destabilized by light activation. PMID: 25274813
There is a correlation between the stability of rhodopsin mutations and disease severity and levels of membrane-bound rhodopsin. PMID: 24520188
Many biochemical studies have demonstrated that P23H mutation induces rhodopsin (RHO) misfolding leading to endoplasmic reticulum stress. PMID: 24664733
These studies indicate that activation of either IRE1, ATF6, or PERK prevents mutant rhodopsin from accumulating in the cells. PMID: 24664756
It regulates relaxation of vascular smooth muscle. PMID: 24717605
In the dark, rhodopsin 11-cis retinal chromophore serves as an inverse agonist to lock the receptor in an inactive state. (Review) PMID: 24183693
development of rod photoreceptors in TgP23H swine embryos. PMID: 24618321
Retinitis pigmentosa mutants provide insight into the role of the N-terminal cap in rhodopsin folding, structure, and function. PMID: 24106275
This study demonistrated that rhodopsin P23H mutation cause early degeneration of retin. PMID: 23557623
The purpose of this study was to test for mechanisms by which the autosomal dominant rhodopsin mutation Ter349Glu causes an early, rapid retinal degeneration. PMID: 23940033
X-ray crstallographic analysis of rhodopsin reveals the congenital stationary night blindness-causing G90D mutation introduces a salt bridge with K296. PMID: 23579341
The S186W mutant thermally destabilizes rhodopsin by disrupting a hydrogen bond network at the receptor's active site. PMID: 23625926
The c.233A>T mutation at RHO exon 1 caused sectorial retinitis pigmentosa in a pedigree with intrafamilial clinical heterogeneity. PMID: 23402891
Two mutations in the RHO gene have been found in two Chinese families with retinitis pigmentosa. PMID: 23288993
Pathogenic mutations in rhodopsin can lead to autosomal dominant retinitis pigmentosa. PMID: 22791210
Data suggest that BiP (HSPA5) is important for maintaining the solubility of rod opsin in the endoplasmic reticulum. PMID: 22855534
Less severe phenotypes occurred in patients with p.R135W in rhodopsin. PMID: 23049240

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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