Recombinant Human Interferon-Induced Protein With Tetratricopeptide Repeats 3 (IFIT3) Protein (His-SUMO)

Name: Recombinant Human Interferon-Induced Protein With Tetratricopeptide Repeats 3 (IFIT3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09912P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Interferon-Induced Protein With Tetratricopeptide Repeats 3 (IFIT3) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O14879
Target Symbol	IFIT3
Synonyms	CIG 49; CIG49; GARG 49; IFI-60K; IFI60; IFI60K; IFIT-3; IFIT-4; Ifit3; IFIT3_HUMAN; IFIT4; Interferon induced 60 kDa protein; Interferon induced protein 60; Interferon induced protein with tetratricopeptide repeats 3; Interferon-induced 60 kDa protein; Interferon-induced protein with tetratricopeptide repeats 3; Interferon-induced protein with tetratricopeptide repeats 4; IRG2; ISG-60; ISG60; P60; Retinoic acid induced gene G protein; Retinoic acid-induced gene G protein; RIG G; RIG-G; RIGG; RP11-149I23.4
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSEVTKNSLEKILPQLKCHFTWNLFKEDSVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYAWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNHPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKSPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNKALEKGLNPLNAYSDLAEFLETECYQTPFNKEVPDAEKQQSHQRYCNLQKYNGKSEDTAVQHGLEGLSISKKSTDKEEIKDQPQNVSENLLPQNAPNYWYLQGLIHKQNGDLLQAAKCYEKELGRLLRDAPSGIGSIFLSASELEDGSEEMGQGAVSSSPRELLSNSEQLN
Expression Range	1-490aa
Protein Length	Full Length
Mol. Weight	72.0kDa
Research Area	Immunology
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	IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exhibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Upregulates CDKN1A/p21 by downregulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2.
Subcellular Location	Cytoplasm. Mitochondrion.
Protein Families	IFIT family
Database References	HGNC: 5411 OMIM: 604650 KEGG: hsa:3437 STRING: 9606.ENSP00000360876 UniGene: Hs.47338
Tissue Specificity	Expression significantly higher in peripheral blood mononuclear cells (PBMCs) and monocytes from systemic lupus erythematosus (SLE) patients than in those from healthy individuals (at protein level). Spleen, lung, leukocytes, lymph nodes, placenta, bone m

Gene Functions References

We provided the evidence that IFIT3 was up-regulated during hepatic ischemia-reperfusion injury (IRI) and knockdown of IFIT3 exerted potent protective effects against hepatic IRI in vitro and in vivo. Our findings not only revealed the mechanism for IFIT3-regulated hepatic IRI, but also proposed potential clinical significance of treatment targeting IFIT3 for patients undergoing liver resection and liver transplantation. PMID: 29734133
These findings indicated that hepatitis B virus-induced miR146a attenuates cell-intrinsic anti-viral innate immunity through targeting RIG-I and RIG-G. PMID: 27210312
Low RIG-G expression is associated with lung cancer. PMID: 27602766
Biomarker expression in pancreatic ductal adenocarcinoma (PDAC) of CXCR4, SMAD4, SOX9 and IFIT3 will be prospectively assessed by immunohistochemistry and verified by rt.-PCR from tumor and adjacent healthy pancreatic tissue of surgical specimen. PMID: 28356064
these data suggest that postpartum, the normalization of the physiological rheostat controlling IFN signaling depends on IFNL3 genotype. PMID: 27601663
Higher expression of IFIT3 enhances anti-apoptotic activity and chemotherapy resistance of pancreatic ductal adenocarcinoma cells. High expression of IFIT3 was independently correlated to shorter patients' survival and may serve as a prognostic marker. PMID: 28210844
Among the associated variants were two in regions previously unreported for COPD; a low frequency non-synonymous SNP in MOCS3 (rs7269297, pdiscovery=3.08x10(-6), preplication=0.019) and a rare SNP in IFIT3, which emerged in the meta-analysis (rs140549288, pmeta=8.56x10(-6)). PMID: 26917578
HSV-1 was shown for the first time to evade the antiviral function of IFIT3 via UL41. PMID: 27681138
results indicated that RIG-G level was high in maturated cells and low in blast cells, and suggested that RIG-G might play a role in the differentiation of bone marrow hemocytes in vivo PMID: 26686474
The transcription factor SOX9, which is linked to regulation of hypoxia-related genes, was identified as a key mediator of upregulation of the oncogene IFIT3 and thereby sustaining a "pseudoinflammatory" cellular condition in pancreatic tumors. PMID: 25650658
Reovirus T3D infection induced STAT-1, ISG-15, IFIT-1, Mx1 and IFIT-3 expression. PMID: 25905045
In cell models of dengue virus 2 infection, authors found that IFITM3 contributed to both the baseline and interferon-induced inhibition of virus entry. PMID: 25131332
protective roles of IFIT3 following IFN-alpha production in DV infection of human lung epithelial cells PMID: 24223959
these findings reveal for the first time the negative regulation of Rig-G on SCF-E3 ligase activities through disrupting CSN complex, not only contributing to further investigation on biological functions of Rig-G, but also leading to better understanding of the CSN complex as a potential target in tumor diagnosis and treatment. PMID: 23415865
RIG-G gene expression is closely correlated with the cross-talk between all-trans retinoic acid and IFN-alpha-induced signaling pathways in NB4 tumor cells. PMID: 22490698
our study characterizes IFIT3 as an important modulator in innate immunity PMID: 21813773
All-trans retinoic acid upregulated RIG-G in NB4 cells by upregulating IRF1, IRF9 and STAT2. PMID: 20137113
The complex STAT2/IRF-9 is the key factor mediating the expression of RIG-G gene regulated by IFN-alpha. PMID: 20403236
concluded that the expression of RIG-G was independent on the classical JAK-STAT pathway, but could be greatly increased by it. PMID: 21056555
Identification of alpha interferon-induced genes associated with antiviral activity in Daudi cells and characterization of IFIT3 as a novel antiviral gene. PMID: 20686046
transcription factors for the reporter gene. CONCLUSION: Both ISRE I and ISRE II on the RIG-G promoter are the binding sites for the complex of transcription factors. They are required for RIG-G expression, and ISRE I has a preferential role over ISRE II. PMID: 20533260
The induction of IFIT4 transcription by IFN-alpha depends upon sequential activation of PKCdelta, JNK and STAT1, and the influence of PKCdelta or JNK on IFN-alpha-mediated induction of IFIT4 is dependent upon the phosphorylation of STAT1 at Ser-727. PMID: 17933493
IFIT4 may play roles in promoting monocyte differentiation into dendritic cell-like cells (DCLCs) and in directing DCLCs to modulate T-helper-1 cell differentiation, thus contributing to the autoimmunity and pathogenesis of systemic lupus erythematosus. PMID: 18706081
Induction of RIG-G by retinoic acid in NB4 cells resulted, to some extent, from an IFNalpha autocrine pathway, a finding that suggests a novel mechanism for the signal cross-talk between IFNalpha and retinoic acid. PMID: 19351818

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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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