Recombinant Human Interferon Regulatory Factor 1 (IRF1) Protein (His-HA)

Beta LifeScience SKU/CAT #: BLC-11020P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Interferon Regulatory Factor 1 (IRF1) Protein (His-HA)

Beta LifeScience SKU/CAT #: BLC-11020P
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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description Recombinant Human Interferon Regulatory Factor 1 (IRF1) Protein (His-HA) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P10914
Target Symbol IRF1
Synonyms Interferon regulatory factor 1; Interferon regulatory factor 1 isoform +I9; Interferon regulatory factor 1 isoform d78; Interferon regulatory factor 1 isoform delta4; Interferon regulatory factor 1 isoform delta7; IRF 1; IRF-1; IRF1; IRF1_HUMAN; MAR; MAR1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His-HA
Target Protein Sequence MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKSKAKRKSCGDSSPDTFSDGLSSSTLPDDHSSYTVPGYMQDLEVEQALTPALSPCAVSSTLPDWHIPVEVVPDSTSDLYNFQVSPMPSTSEATTDEDEEGKLPEDIMKLLEQSEWQPTNVDGKGYLLNEPGVQPTSVYGDFSCKEEPEIDSPGGDIGLSLQRVFTDLKNMDATWLDSLLTPVRLPSIQAIPCAP
Expression Range 1-325aa
Protein Length Full Length
Mol. Weight 43.6 kDa
Research Area Cardiovascular
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.
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 Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. Regulates transcription of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters. Competes with the transcriptional repressor ZBED2 for binding to a common consensus sequence in gene promoters. Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, ZBP1, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA; metabolic enzymes, such as ACOD1/IRG1. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells.
Subcellular Location Nucleus. Cytoplasm.
Protein Families IRF family
Database References
Associated Diseases Gastric cancer (GASC)

Gene Functions References

  1. IRF-1 regulates Rab27a transcription and extracellular vesicles secretion, leading to oxidized phospholipids activation of neutrophils and subsequent hepatic IR injury PMID: 29059701
  2. Down-regulation of interferon regulatory factor 1 gene expression in hepatitis B virus patients without rejection emphasized counteraction between hepatitis B virus replication and interferon regulatory factor 1 production. On the other hand, interferon regulatory factor 1 gene overexpression in patients with rejection may result in inflammatory reactions and ischemic-reperfusion injury. PMID: 27310137
  3. IRF-1 polymorphisms influence the risk for childhood allergic asthma being associated with increased pro-inflammatory gene regulation. PMID: 29047170
  4. IRF1 served as tumor suppressor in the regulation of cholangiocarcinoma cells proliferation, cell cycle, migration and invasion PMID: 29107934
  5. this study shows that IRF-1 is a regulator of lipopolysaccharide -induced endothelial proinflammatory activation PMID: 28658674
  6. These results revealed that IRF-1 is involved in the IFN-inducible expression of Nmi. PMID: 28913576
  7. our results indicated that IL-1beta treatment resulted in a significant increase in expression of the transcriptional factor interferon regulatory factor-1 (IRF-1) at both the mRNA and protein levels, which was significantly ameliorated by treatment with Nebivolol. The combination of these findings suggests that Nebivolol can potentially be applied in human osteoarthritis treatment PMID: 28512729
  8. The authors observe that IRF1 expression is mediated by ZEB1 de-repression, and the study demonstrates how airway remodelling/fibrosis is associated with a defective mucosal antiviral response through ZEB1-initiated epigenetic silencing in respiratory virus infection. PMID: 28581456
  9. These unprecedented data suggest that IRF1 and NF-kappaB orchestrate the TLR4-primed immunomodulatory response of hMSCs and that this response also involves the PI3K pathway. PMID: 27444640
  10. Zinc is capable of ameliorating the allogeneic immune reaction by enhancement of antigen-specific iTreg cells due to modulation of essential molecular targets by upregulation of Foxp3 and KLF-10 and downregulation of IRF-1. PMID: 27260002
  11. As a measure of PD-L1 expression capability, IRF-1 expression may be a more valuable predictive biomarker for anti-PD-1 therapy than PD-L1 itself. PMID: 28331615
  12. Upregulation of IRF1 in human adipocytes leads to phenotypes associated with obesity-related inflammation. PMID: 28416283
  13. Regulation of transcriptional activators by DNA-binding domain (DBD) ubiquitination has shown that, when attached to the DBD of either p53 or IRF-1, ubiquitin is orientated towards, and makes contact with, the DNA. PMID: 28362432
  14. In SK-Hep1 cells, an increase in apoptosis and decrease in autophagy were observed after IFN-gamma stimulation, which was accompanied with increasing IRF-1 levels. PMID: 27191889
  15. HNP1 upregulation of cytokine expression in pDCs was inhibited by blockade of NF-kappaB activation or knockdown of IRF1, demonstrating the importance of these two signaling events in HNP1-induced pDC activation. PMID: 27031443
  16. Data show that the Japanese encephalitis virus (JEV)-induced expression of miR-301a led to inhibition of the production of the transcription factor IFN regulatory factor 1 (IRF1) and the signaling protein suppressor of cytokine signaling 5 (SOCS5). PMID: 28196914
  17. A comprehensive mass spectrometric analysis identified interferon regulatory factor 1 (IRF1) as a key transcription factor in growth arrest of LNCaP-mTOR. PMID: 28905415
  18. our data provide an important insight into STING-mediated induction of type I and III IFNs and subsequent antiviral signaling pathways that regulate VZV replication in human dermal cells. PMID: 28647346
  19. IFN regulatory factor 1 effectively inhibits hepatitis E virus replication through the activation of the JAK-STAT pathway PMID: 27328944
  20. B. abortus lipoproteins via IL-6 inhibit the expression of IFN regulatory factor 1 (IRF-1), a critical regulatory transcription factor for CIITA induction. PMID: 27765819
  21. STAT1 and IRF1 collaborate to induce interferon-gamma stimulated genes (ISGs), but the extent to which they act alone or together is unclear.This study provides strong evidence for widespread cooperation between STAT1 and IRF1 at ISGs, and suggests that in silico predictions reliably predict the effect of nucleotide variants on binding in vivo. PMID: 28274199
  22. aimed to determine the role of Treg cells and IRF-1 in MDS PMID: 28113084
  23. Tat exploited the cellular HDM2 (human double minute 2 protein) ubiquitin ligase to accelerate IRF-1 proteasome-mediated degradation, resulting in a quenching of IRF-1 transcriptional activity during HIV-1 infection. PMID: 27795392
  24. Leading to a STAT1-IRF1 controlled upregulation of TLR3 expression in macrophages. PMID: 27940139
  25. Regulatory elements for both IRF-1 (-1019 to -1016) and CREB (-1198 to -1195), specific to the distal THBS1 promoter, were required for leptin-induced TSP-1 transcription. PMID: 27281481
  26. Inflammation-driven IRF1 and NF-kappaB activity promotes ERVK reactivation. PMID: 27512062
  27. MiR-23a downregulates the expression of IRF-1 in HCC cells. PMID: 27279136
  28. the interactions of IRF1, IFN-beta and IRF5 are involved in the M1 polarization of macrophages and have antitumor functions. PMID: 27176664
  29. rs56288038 (C/G) in IRF-1 3'UTR acted as a promotion factor in gastric cancer development through enhancing the regulatory role of miR-502-5p in IRF-1 expression. PMID: 27866197
  30. An IRF-1 shorter splicing transcript has been identified in acute promyelocytic leukemia cells dispalying similar transactivation activity to the full length transcript. PMID: 28039033
  31. Data suggest that interferon beta (IFN-beta) might be involved in modulating the expressions of interferon regulatory factor 1 (IRF1) and interferon regulatory factor-5 protein (IRF5) as well as maintaining the M1 polarization status and its function. PMID: 27363262
  32. IRF1 upregulation in fetal membranes and myometrium after term labor indicates a proinflammatory role for IRF1 in human parturition. IRF1 is involved in TLR- and cytokine-mediated signaling in human myometrium. PMID: 26674566
  33. 5AZ had a protective effect after MI by potentiation of IRF1 sumoylation and is suggested as a novel therapeutic intervention for cardiac repair. PMID: 26510961
  34. IRF1 is a transcriptional regulator of IRG1 in human macrophages. PMID: 26872335
  35. Data show that ectopic expression of interferon regulatory factor 1 (IRF-1) reduces NF-kappa B activity and suppresses TNF receptor-associated factor 2 (TRAF2) and inhibitor of apoptosis 1 protein (cIAP1) expression in breast cancer cells. PMID: 26011589
  36. Gene expression meta-analysis reveals immune response convergence on the IFNgamma-STAT1-IRF1 axis and adaptive immune resistance mechanisms in lymphoma PMID: 26362649
  37. The present data demonstrate that IRF-1 could effectively promote the immune maturation and function of dendritic cells in ACS Acute Coronary Syndrome patients. PMID: 25997853
  38. IRF1, a transcription factor, regulates miR-203 transcription by binding to the miR-203 promoter. PMID: 25658920
  39. Single nucleotide polymorphisms in RBPJ, IL1R1, REV3L, TRAF3IP2, IRF1 and ICOS showed association with rheumatoid arthritis in black South Africans. PMID: 25014791
  40. IRF1 directly interacts with chromatin modifying enzymes, supporting a model where recruitment to specific target genes is mediated in part by IRF1. PMID: 25611806
  41. IRF1 re-expression in human cancer cells causes cells to become resistant to infection by the oncolytic vesicular stomatitis virus strain. PMID: 25347735
  42. IRF1 is a dual regulator of BV6-induced apoptosis and inflammatory cytokine secretion. PMID: 25501823
  43. IRF-1 promotes LTx I/R injury via hepatocyte IL-15/IL-15Ralpha production and suggest that targeting IRF-1 and IL-15/IL-15Ralpha may be effective in reducing I/R injury associated with LTx. PMID: 25964490
  44. IRF-1 regulates the transcription of target genes which play essential roles in various physiological and pathological processes, including viral infection, tumor immune surveillance, pro-inflammatory injury, development of immune system. (Review) PMID: 25312803
  45. silencing IRF1 promoted autophagy by increasing BECN1 and blunting IGF1 receptor and mTOR survival signaling PMID: 25576084
  46. IRF-1 is an important signaling protein in the interferon pathway. It not only activates gene expression as a transcription factor, but may perpetuate disease by leading to a dysregulated epigenome PMID: 25418955
  47. Data suggest that interferon regulatory factors 1 and 2 (IRF1 and IRF2) may serve as potential targets of therapy. PMID: 24632547
  48. Data indicate that the interferon regulatory factor (IRF1) promotion was observed in cancer cell lines treated with different MEK inhibitors or with RNAi oligonucleotides against extracellular signal-regulated kinases (ERK1/2). PMID: 25497010
  49. A positive feedback loop between IRF1 and miR-29b may contribute to the sensitivity of colorectal cancer cells to IFN-gamma by repressing IGF1. PMID: 25592039
  50. The novel AS regulatory activities attributed to IRF-1 indicate that the IFN-gamma response involves a global change in both gene transcription and AS in breast epithelial cells. PMID: 24650050

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

More from Cytokines
Recently viewed