Recombinant Human S-Arrestin (SAG) Protein (His)

Name: Recombinant Human S-Arrestin (SAG) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03368P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) SAG.

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Product Overview

Description	Recombinant Human S-Arrestin (SAG) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P10523
Target Symbol	SAG
Synonyms	48 kDa protein; Arrestin 1; Arrestin; ARRS_HUMAN; Retinal S antigen (48 KDa protein); Retinal S-antigen; Rod photoreceptor arrestin; RP47; S antigen; S antigen retina and pineal gland (arrestin); S arrestin; S-AG; S-arrestin; SAG
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MAASGKTSKSEPNHVIFKKISRDKSVTIYLGNRDYIDHVSQVQPVDGVVLVDPDLVKGKKVYVTLTCAFRYGQEDIDVIGLTFRRDLYFSRVQVYPPVGAASTPTKLQESLLKKLGSNTYPFLLTFPDYLPCSVMLQPAPQDSGKSCGVDFEVKAFATDSTDAEEDKIPKKSSVRLLIRKVQHAPLEMGPQPRAEAAWQFFMSDKPLHLAVSLNKEIYFHGEPIPVTVTVTNNTEKTVKKIKAFVEQVANVVLYSSDYYVKPVAMEEAQEKVPPNSTLTKTLTLLPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVLGILVSYQIKVKLTVSGFLGELTSSEVATEVPFRLMHPQPEDPAKESYQDANLVFEEFARHNLKDAGEAEEGKRDKNDVDE
Expression Range	1-405aa
Protein Length	Full Length
Mol. Weight	47.1kDa
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	Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO. May play a role in preventing light-dependent degeneration of retinal photoreceptor cells.
Subcellular Location	Cell projection, cilium, photoreceptor outer segment. Membrane; Peripheral membrane protein.
Protein Families	Arrestin family
Database References	HGNC: 10521 OMIM: 181031 KEGG: hsa:6295 STRING: 9606.ENSP00000386444 UniGene: Hs.32721
Associated Diseases	Night blindness, congenital stationary, Oguchi type 1 (CSNBO1); Retinitis pigmentosa 47 (RP47)
Tissue Specificity	Detected in retina, in the proximal portion of the outer segment of rod photoreceptor cells (at protein level).

Gene Functions References

This is the first dominant-acting mutation identified in SAG, a founder mutation possibly originating in Mexico several centuries ago. The phenotype is clearly adRP and is distinct from the previously reported phenotypes of recessive null mutations, that is, Oguchi disease and recessive RP. PMID: 28549094
Macular dysfunction can occur in Oguchi disease with the 1147delA mutation in the SAG gene. PMID: 21447990
Based on their observed affinity for arrestin-1, P-opsin and inactive P-Rh very likely affect the physiological monomer-dimer-tetramer equilibrium of arrestin-1, and should therefore be taken into account when modeling photoreceptor function. PMID: 23277586
Compound heterozygosity of a nonsense R193X mutation and a heterozygous deletion of 3,224 bp encompassing exon 2 in the SAG gene is the cause of Oguchi's disease in a Chinese family. PMID: 22419846
the arrestin 1147delA, which has been known as a frequent cause of Oguchi disease, also may be related to the pathogenesis of autosomal recessive RP. PMID: 21922265
We describe a case of Oguchi disease with unusual findings caused by a putative heterozygous mutation in the SAG gene. PMID: 21987685
maintenance of low levels of the active monomer is the biological role of arrestin-1 self-association PMID: 21288033
Rhodopsin-arrestin complexes alter the morphology of endosomal compartments and severely damage receptor-mediated endocytic functions in retinitis pigmentosa. PMID: 15232620
The existence of 2 novel mutations of the arrestin gene in 2 unrelated Japanese patients strongly supports the previous data that arrestin gene mutations are associated with Oguchi's disease PMID: 15234147
Mutation 926delA of the SAG gene is the main cause of Oguchi disease in Japanese. This mutation appears to have been inherited from a single founder. PMID: 15295660
The tetramer form of arrestin increases the arrestin-binding capacity of microtubules while readily dissociating to supply active monomer when it is needed to quench rhodopsin signaling. PMID: 17332750
ARRESTIN binds to different phosphorylated regions of the thyrotropin-releasing hormone receptor with distinct functional consequences. PMID: 18413662
S-Ag specific T cells are present in certain active Behcet's disease patients, and most of them are activated memory CD4(+) T cells. PMID: 18685727

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.