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

Beta LifeScience SKU/CAT #: BLC-07966P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

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

Beta LifeScience SKU/CAT #: BLC-07966P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Mouse S-Arrestin (SAG) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P20443
Target Symbol SAG
Synonyms Sag; S-arrestin; 48 kDa protein; Retinal S-antigen; S-AG; Rod photoreceptor arrestin
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence MAACGKTNKSHVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLYFSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKIPKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLNLSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQIANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSEVATEVPFRLMHPQPEDPAKESVQDENLVFEEFARQNLKDTGENTEGKKDEDAGQDE
Expression Range 1-403aa
Protein Length Full Length
Mol. Weight 50.4 kDa
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
Tissue Specificity Detected in retina (at protein level).

Gene Functions References

  1. We conclude that, in addition to their well-established roles in Meta II inactivation, Grk1 and Arr1 can modulate the kinetics of Meta III decay and rod dark adaptation in vivo. PMID: 27353443
  2. The G-protein coupled receptor, DRD4, requires ARR1 and ARR4 for desensitization and internalization. PMID: 26169958
  3. ARR4 modulates essential functions in high acuity vision and downstream cellular signaling pathways that are not fulfilled or substituted by the coexpression of ARR1, despite its high expression levels in all mouse cones. PMID: 26284544
  4. 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
  5. Sag is essential for embryonic vasculogenesis and tumor angiogenesis. PMID: 24213570
  6. SAG knockdown caused the accumulation of proapoptotic Bax and SARM, imbalance of Bcl-2/Bax in the mitochondria, induction of cytosolic cytochrome c and activation of caspases, all of which led to disequilibrium between life and death of macrophages. PMID: 24786833
  7. tetrameric visual arrestin 1 is a biomarker for retinal function in diabetic mice, assessed by MRI PMID: 25351983
  8. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. PMID: 24012956
  9. Findings suggest a role for Bardet-Biedl syndrome 5 (BBS5) in regulating light-dependent translocation of arrestin1 (Arr1). PMID: 23817741
  10. Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina. PMID: 23690606
  11. the 139-loop stabilizes basal conformation of arrestin-1 and acts as a brake, preventing its binding to non-preferred forms of rhodopsin. PMID: 23476014
  12. a novel function of palmitoylation in shaping subcellular cAMP-PKA signaling in cardiomyocytes via modulating the recruitment of beta arrestin 2-PDE4D complexes to the agonist-stimulated beta(2)AR PMID: 22912718
  13. Photoresponse recovery rates of mice with arrestin-1 content in the outer segment, were measured. PMID: 21818392
  14. Physiological level of arrestin-1 expression in rods reflects the balance between short-term functional performance of photoreceptors and their long-term health. PMID: 21075174
  15. maintenance of low levels of the active monomer is the biological role of arrestin-1 self-association PMID: 21288033
  16. siRNA silencing induces radiosensitization by increasing ROS levels and blocking NF-kappaB activation PMID: 20638939
  17. study demonstrates a vital alternative function for Arr1 in the photoreceptor synapse and provides key insights into the potential molecular mechanisms of inherited retinal diseases, such as Oguchi disease and Arr1-associated retinitis pigmentosa. PMID: 20631167
  18. Prolonged illumination up-regulates retinal arrestin and Guca1a/b: a novel mechanism for light adaptation. PMID: 19332500

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.

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