Recombinant Human Sulfiredoxin-1 (SRXN1) Protein (His&Myc)

Name: Recombinant Human Sulfiredoxin-1 (SRXN1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01057P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Sulfiredoxin-1 (SRXN1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9BYN0
Target Symbol	SRXN1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MGLRAGGTLGRAGAGRGAPEGPGPSGGAQGGSIHSGRIAAVHNVPLSVLIRPLPSVLDPAKVQSLVDTIREDPDSVPPIDVLWIKGAQGGDYFYSFGGCHRYAAYQQLQRETIPAKLVQS
Expression Range	1-137aa
Protein Length	Full Length
Mol. Weight	19.9 kDa
Research Area	Cell Biology
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	Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.
Subcellular Location	Cytoplasm.
Protein Families	Sulfiredoxin family
Database References	HGNC: 16132 OMIM: 617583 KEGG: hsa:140809 STRING: 9606.ENSP00000371388 UniGene: PMID: 29441509 Study identify a role for Srxn1 as a denitrosylase for neuronal Prx2. Finding points to the NO/Srxn1 pair in a previously unrecognized redox cycle that modulates Prx2 peroxidase activity. PMID: 27821734 Wnt/beta-catenin pathway was stimulated by sulfiredoxin in tumor cell line, with activation of CD44-its target genes-resulting in the promotion of invasion and migration in cervical cancer cell lines. PMID: 28448437 This review will highlight the cumulative effects of sulfiredoxin in various systemic disorders with a strong emphasis on its target activity and the factors influencing its expression in such conditions. PMID: 25460739 The up-regulated expression of Srx was significantly associated with lymph node metastasis, infiltration of vessels, and the depth of cancer invasion. PMID: 28274319 The analysis of SXR polymorphism is a promising tool to predict both the favourable response to corticosteroids and the risk of developing steroid resistance PMID: 27377607 rs6053666 of SRXN1 is associated with cerebrovascular disease in a Finnish cohort PMID: 27226772 Increased expression of Srx protects peroxiredoxins against hyperoxidation in the early stage of hyperglycaemia. PMID: 28202395 We silenced Srx by short hairpin RNA in HeLa and SiHa cells. Diminished Srx expression upregulated E-cadherin expression. The cell invasion and migration activity in the ShSrx group were obviously decreased in HeLa and SiHa cells. PMID: 28351308 Study shows that Srx plays a critical oncogenic role to promote cell invasion and metastasis, which is at least partially due to its stimulation of the MAPK pathway through EGFR deacetylation. PMID: 26290602 This review will summarize the molecular basis of differences in the affinity of Srx for individual Prx and the role of individual component of the Srx-Prx system in tumor progression and metastasis. PMID: 26170166 Gemfibrozil, a lipid-lowering drug, increases myelin genes in human oligodendrocytes via peroxisome proliferator-activated receptor-beta. PMID: 22879602 NRF2 and SRXN1 genetic polymorphisms are associated with breast cancer risk and survival PMID: 22964583 SRX forms a complex with S100A4 (and has stronger affinity for S-glutathionylated S100A4), regulates its activity, and mediates redox regulation of the interaction of S100A4 with nonmuscle myosin heavy chain II-A. PMID: 22934964 Smokers and ex-smokers had significantly more sulfiredoxin expression in their tumors and in patients receiving cytostatic drugs or radiation therapy, sulfiredoxin expression predicted a poor prognosis. PMID: 21943684 Srx functions as a novel component to maintain the balance between H2O2 production and elimination PMID: 22086924 Srx-Prx IV axis is critical for lung cancer maintenance and metastasis, suggesting that targeting the Srx-Prx IV axis may provide unique effective strategies for cancer prevention and treatment. PMID: 21487000 sulfiredoxin 1 is associatd with the pathogenesis of human pulmonary fibrosis. PMID: 20718723 Studies present the 2.1 A crystal structure of human Srx in complex with PrxI, ATP, and Mg(2+). PMID: 19812042 The reduction of the cysteine sulfinic acid moiety within the active site of the peroxiredoxin by sulfiredoxin involves novel sulfur chemistry and the use of ATP and Mg(2+). PMID: 15952770 analysis of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin PMID: 16565085 Actin and protein tyrosine phosphatase 1B were identified in vitro as targets of sulfiredoxin 1 (Srx1)-dependent deglutathionylation. PMID: 16818657 Aspartate-187 of peroxiredoxin (Prx) I is the catalytic residue responsible for ATP hydrolysis in the cysteinesulfinic acid reduction of Prx by human sulfiredoxin. PMID: 17176052 2.6 A crystal structure of the human Srx-PrxI complex [Srx] PMID: 18172504 Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate PMID: 18579529 analysis of a protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin PMID: 18593714 decreased expression in lungs from patients with chronic obstructive pulmonary disorder PMID: 19027064 The current study identifies Sulfiredoxin as a unique target of activator protein-1 (AP-1) activation and TAM67 inhibition. PMID: 19057013 Deglutathionylation of 2-Cys Prx is specifically catalyzed by Srx. PMID: 19561357

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.