Recombinant Pig Rhodopsin Protein (Tagged)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Pig
Accession	O18766
Synonym	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
Description	Recombinant Pig Rhodopsin Protein (Tagged) was expressed in Mammalian. It is a Protein fragment
Source	Mammalian
AA Sequence	MNGTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQ
Molecular Weight	38 kDa
Purity	>85% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilised
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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 11-cis 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	KEGG: ssc:397437 STRING: 9823.ENSSSCP00000012353 UniGene: Ssc.16150

Gene Functions References

the rhodopsin is densely packed in the retina and the rhodopsin molecules are not aligned well. PMID: 22842041
Phototransduction, even when initiated by wild type rhodopsin, is altered in a way progressive with level of retinal degeneration. A model introduces idea of binding site for carboxy terminus of rhodopsin on rhodopsin kinase. PMID: 16402026

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.