Recombinant Human Interferon-Induced Transmembrane Protein 1 (IFITM1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03617P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Interferon-Induced Transmembrane Protein 1 (IFITM1) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-03617P
Regular price $398.00 Sale price $349.00Save $49
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Product Overview

Description Recombinant Human Interferon-Induced Transmembrane Protein 1 (IFITM1) Protein (GST) is produced by our E.coli expression system. This is a extracellular protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P13164
Target Symbol IFITM1
Synonyms 9-27; CD 225 ; CD 225 antigen; CD225; CD225 antigen; Dispanin subfamily A member 2a; DSPA2a; IFI 17; IFI17; IFITM1; IFM1_HUMAN; Interferon induced protein 17; interferon induced transmembrane protein 1 (9-27); Interferon induced transmembrane protein 1; Interferon inducible protein 9-27; Interferon-induced protein 17; Interferon-induced transmembrane protein 1; Interferon-inducible protein 9-27; Leu 13; Leu 13 antigen; Leu-13 antigen; LEU13
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MHKEEHEVAVLGPPPSTILPRSTVINIHSETSVPDH
Expression Range 1-36AA
Protein Length Extracellular Domain
Mol. Weight 31.0kDa
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 inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV and SARS-CoV-2 S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Inhibits SARS-CoV-2 S protein-mediated syncytia formation. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation. IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome.
Subcellular Location Cell membrane; Single-pass membrane protein. Lysosome membrane.
Protein Families CD225/Dispanin family
Database References
Tissue Specificity Bone (at protein level). Levels greatly elevated in colon cancer, cervical cancer, esophageal cancer and ovarian cancer. Expressed in glioma cell lines.

Gene Functions References

  1. Strong ifitm1 Expression in CD4 T Cells in HIV Controllers Is Correlated With Immune Activation PMID: 27552157
  2. Using a multi-group heat map from GSE9716 analysis of the GEO database, IFITM1 was determined to be a relevant radioresistance gene. Inhibition of IFITM1 in combination with radiotherapy could, indeed, inhibit oral neoplasm cells. PMID: 29770536
  3. Inactivated viral particle inoculation increased the expression of IFITM1protein at mRNA and protein levels, and mediated the antiviral state in HUVECs. PMID: 29100522
  4. Identification of three distinct mutations that converted IFITM1 or IFITM3 from inhibitors to enhancers of MERS-CoV or SARS-CoV spike protein-mediated entry revealed key structural motifs or residues determining the biological activities of IFITM proteins. PMID: 29263263
  5. Epithelial-mesenchymal transition (EMT) signature was dysregulated by both loss and gain of function of IFITM1, which was partially reverted by Caveolin-1 (CAV1). PMID: 27852071
  6. These results indicate that IFITM1 protein can restrict alphavirus infection by inhibiting viral fusion with cellular membranes. PMID: 27219333
  7. The transcriptional regulation of IFITM1, 2 and 3 expression. PMID: 28511927
  8. IFITM1 and IFITM3 inhibit Zika virus infection early in the viral life cycle. PMID: 27268505
  9. IFITM1 suppression blocks proliferation and invasion of aromatase inhibitor-resistant breast cancer in vivo by JAK/STAT1-mediated induction of p21. PMID: 28411130
  10. Compared with CD10, IFITM1 has superior performance distinguishing endometrial stroma of adenomyosis from mesenchyma surrounding invasive endometrial adenocarcinoma. PMID: 27124937
  11. Overexpression of IFITM1 is associated with Oral Squamous Cell Carcinomas. PMID: 27221933
  12. High expression of IFITM1 is associated with poor prognosis of colorectal cancer. PMID: 26884876
  13. These findings indicate that overexpression of IFITM1 enhances the aggressive phenotype of triple-negative SUM149 IBC cells and that this effect is dependent on STAT2/BRG1 interaction. PMID: 26897526
  14. propose that the IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation and demonstrate that the actions of the IFITM proteins are indeed virus and cell-type specific PMID: 26354436
  15. the importance of the C-terminal region of IFITM1 in modulating the antiviral function through controlling protein subcellular localization. PMID: 25738301
  16. Suggest that IFITM1 promotes the aggressiveness of colorectal cancer cells via caveolin-1 signaling. PMID: 26259513
  17. In virus-producing cells, IFITMs coalesce with forming virions and are incorporated into HIV-1 viral particles. PMID: 25422070
  18. Incorporation of IFITM1, IFITM2 and IFITM3 into HIV-1 virions impair viral fusion and spread. PMID: 25464829
  19. Host IFITM3,IFITM2 and IFITM1 facilitate morphogenesis of the human cytomegalovirus assembly. PMID: 25552713
  20. Schizophrenia subjects with higher IFITM mRNA levels in cortical blood vessels have greater disturbances in cortical GABA neurons suggests that these cell-type disturbances might be influenced by a shared upstream insult that involves immune activation. PMID: 24209773
  21. IFITM1 could be a novel metastasis-promoting gene that enhances the metastatic phenotype in ovarian cancer via epigenetic transcriptional regulation. PMID: 24676393
  22. IFITM1 is a potential valuable addition to immunohistochemical panels used in the diagnosis of cellular mesenchymal uterine tumors. PMID: 24072182
  23. Results suggest that the g.-1920G>A polymorphism in interferon inducible transmembrane protein 1 (IFITM1) may be associated with susceptibility to ulcerative colitis (UC). PMID: 24120510
  24. IFITM1 is essential for the formation of functional blood vessels and stabilizes EC-EC interactions during endothelial lumen formation by regulating tight junction assembly. PMID: 24603679
  25. Although their inhibitory activities were modest when compared to that of tetherin, IFITMs, but not tetherin, directly reduced the expression of HIV-1 proteins including Gag, Vif and Nef. PMID: 23376165
  26. Authors show that interferon-induced transmembrane protein 1 (IFITM-1), IFITM-2, and IFITM-3 exhibit a broad spectrum of antiviral activity against several members of the Bunyaviridae family. PMID: 23720721
  27. This study defines IFITM1 as an interferon-stimulated gene effector with action against HCV entry. PMID: 22996292
  28. IFITM1 knockdown in human alveolar-derived bone marrow stromal cells was associated with inhibition of Runx2 mRNA and protein expression. PMID: 22634173
  29. Introduction of anti-miR-130a in hepatocytes increased IFITM1 expression. Hepatocytes stably expressing IFITM1 reduced HCV replication. Together, these results suggested that HCV infection of hepatocytes upregulates miR-130a. PMID: 22787204
  30. The results suggest that the expression of IFITM1 controls the invasiveness and migration of gastric cancer. PMID: 22609115
  31. Hepatitis C virus infection suppresses the upregulation of a subset of effector molecules, including ISG56 and IFITM1. PMID: 21976647
  32. IFITM1 was expressed in the five human glioma cell lines, and its expressions were positively correlated with their tumorigenicity PMID: 20838853
  33. IFITM proteins differentially restrict the entry of a broad range of enveloped viruses, and modulate cellular tropism independently of viral receptor expression. PMID: 21253575
  34. IFITM1, IFITM2, and IFITM3 inhibit HIV-1 replication through interfering with virus entry. PMID: 21177806
  35. Data show that ULBP1, TFR2 and IFITM1 were associated with increased susceptibility to Vgamma9Vdelta2 T-cell cytotoxicity. PMID: 20220060
  36. Activated IFITM1 is associated with Peutz-Jeghers syndrome polyps. PMID: 20428811
  37. Down regulation of IFITM1 is associated with cervical squamous cell carcinoma. PMID: 20099975
  38. The positive expression level of IFITM1 is associated with the progression of the carcinogenetic process in Peutz-Jeghers syndrome. PMID: 19304549
  39. LEU13 has a novel role different from that in the inhibition of cell proliferation, involved in IFNA-induced refractoriness of RSa cells to X rays PMID: 12926988
  40. IFITM1 expression profiling could be used for molecular classification of CML, which may also predict survival PMID: 15661263
  41. Overexpression of 9-27 leads to increased migration and invasiveness by suppressing natural killer cells in gastric cancer PMID: 15808405
  42. IFITM1 has a role in cellular sensitivity to CDDP in esophageal cancer PMID: 18202764
  43. IFITM1 plays an important role for the invasion at the early stage of HNSCC progression PMID: 18829488
  44. results revealed that the interaction between IFITM1 and CAV-1 could enhance the inhibitory effect of CAV-1 on ERK activation PMID: 19499152
  45. Antiviral effect of IFITM family members on H1N1 influenza, West Nile virus, and Dengue virus PMID: 20064371

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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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