IFITM1 Antibodies

Structure of IFITM1

IFITM1 is a transmembrane protein with a molecular weight of approximately 14 kDa. Its size varies slightly among different species, mainly due to the conservative variations in the amino acid sequence.

This protein is composed of approximately 125 amino acids and has a typical transmembrane structure, including a highly conserved hydrophobic domain and an intracellular region. Its structural characteristics determine its localization on the cell membrane and endosomal membrane, and it exerts antiviral effects by regulating membrane fluidity and lipid raft functions. The intracellular structure of the protein is involved in signal transduction and mediates the interferon response. The specific amino acid residues in the transmembrane domain of IFITM1 are crucial for its antiviral activity, and mutations at certain conserved sites can significantly affect its ability to inhibit viral invasion.

Fig. 1 IFITM proteins have been described to affect various cancer hallmarks.¹

Key structural characteristics of IFITM1:

• Bifunctional transmembrane domain topology
• Highly conserved CD225 domain
• Palmitoylation modification site
• Membrane localization-related C-terminal region

Functions of IFITM1

The main function of IFITM1 is to mediate the antiviral response of cells and regulate tumor occurrence. However, it is also involved in various physiological and pathological processes, including immune regulation and cell proliferation.

The expression profile of IFITM1 is of a broad-spectrum inducible type. It is rapidly upregulated after interferon stimulation. Unlike constitutively expressed housekeeping genes, its level is relatively low in resting cells, but it sharply increases under viral infection or inflammatory stimulation, demonstrating its functional characteristics as a sentinel of innate immunity.

Applications of IFITM1 and IFITM1 Antibody in Literature

1. Friedlová, Nela, et al. "IFITM protein regulation and functions: Far beyond the fight against viruses." Frontiers in immunology 13 (2022): 1042368. https://doi.org/10.3389/fimmu.2022.1042368

The article indicates that interferon-induced transmembrane proteins (IFITMs) play a significant role in antiviral defense and tumor development. This article reviews the regulatory mechanisms and physiological/pathological functions of IFITM proteins, with a particular focus on their roles in tumor development and anti-tumor immunity.

2. Xu, Rong, et al. "Invasive FoxM1 phosphorylated by PLK1 induces the polarization of tumor-associated macrophages to promote immune escape and metastasis, amplified by IFITM1." Journal of Experimental & Clinical Cancer Research 42.1 (2023): 302. https://doi.org/10.1186/s13046-023-02872-1

The research has found that in lung cancer, PLK1 phosphorylates FoxM1, activates genes such as IFITM1, and promotes macrophage polarization, immune evasion and metastasis. Targeting FoxM1 is expected to become a new strategy for inhibiting the malignant progression of lung cancer.

3. Ishikawa-Sasaki, Kumiko, Takayuki Murata, and Jun Sasaki. "IFITM1 enhances nonenveloped viral RNA replication by facilitating cholesterol transport to the Golgi." PLoS Pathogens 19.5 (2023): e1011383. https://doi.org/10.1371/journal.ppat.1011383

The research found that IFITM1 can promote the transport of cholesterol to the Golgi apparatus, facilitating the accumulation of cholesterol at the RNA replication site of the Iatrophobia virus, thereby enhancing viral replication. This discovery reveals a new mechanism of IFITM1 in the replication of non-enveloped RNA viruses.

4. Kelemen, Andrea, et al. "IFITM1 expression determines extracellular vesicle uptake in colorectal cancer." Cellular and Molecular Life Sciences 78.21-22 (2021): 7009-7024. https://doi.org/10.1007/s00018-021-03949-w

The study found that cells with high expression of IFITM1 in colorectal cancer have strong proliferation ability, but have weak uptake ability for extracellular vesicles (EVs) derived from fibroblasts. This suggests heterogeneity in EV uptake within the tumor, which has significant reference value for cancer treatment strategies based on EVs.

5. Hussein, Hosni AM, et al. "IFITM1 expression is crucial to gammaherpesvirus infection, in vivo." Scientific reports 8.1 (2018): 14105. https://doi.org/10.1038/s41598-018-32350-0

The research has found that IFITM1 promotes the infection of γ-herpesviruses (such as EBV, KSHV), and it functions during the later stage of the virus entering the cells. Animal experiments have confirmed that silencing IFITM1 can significantly reduce the viral titer, indicating that IFITM1 is a key promoting factor for viral infections in the body.

Creative Biolabs: IFITM1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IFITM1 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom IFITM1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our IFITM1 antibodies, custom preparations, or technical support, contact us at email.