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Rabbit Anti-EIF3F Recombinant Antibody (EG1067) (CBMAB-EN1258-LY)

The product is antibody recognizes EIF3F. The antibody EG1067 immunoassay techniques such as: WB: 1:500~1:1000 IHC: 1:50~1:100 ELISA: 1:40000.
See all EIF3F antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse
Clone
EG1067
Antibody Isotype
IgG
Application
WB: 1:500~1:1000 IHC: 1:50~1:100 ELISA: 1:40000

Basic Information

Immunogen
The antibody was produced against synthesized peptide derived from internal of human EIF3F.
Specificity
Human, Mouse
Antibody Isotype
IgG
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Eukaryotic Translation Initiation Factor 3 Subunit F
Introduction
EIF3F (Eukaryotic Translation Initiation Factor 3 Subunit F) is a Protein Coding gene. Among its related pathways are Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S and Viral mRNA Translation. Gene Ontology (GO) annotations related to this gene include thiol-dependent ubiquitin-specific protease activity and translation initiation factor binding. An important paralog of this gene is PSMD7.
Entrez Gene ID
Human8665
Mouse66085
UniProt ID
HumanO00303
MouseQ9DCH4
Alternative Names
Eukaryotic Translation Initiation Factor 3 Subunit F; Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa; Deubiquitinating Enzyme EIF3f; EIF-3-Epsilon; EIF3S5; Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD); Eukaryotic Translation Initiation Factor 3, Subunit F;
Research Area
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815).

The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632).

The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773).

Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.
Biological Process
Formation of cytoplasmic translation initiation complex Source: UniProtKB-UniRule
IRES-dependent viral translational initiation Source: UniProtKB
Protein deubiquitination Source: FlyBase
Translational initiation Source: UniProtKB
Cellular Location
Cytoplasm
Involvement in disease
Intellectual developmental disorder, autosomal recessive 67 (MRT67):
A form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Some MRT67 patients manifest seizures and sensorineural hearing loss.
PTM
Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11.

Nicoli, E. R., Streaţa, I., Yang, J., Macnamara, E., Wolfe, L., Garcia, K., ... & Adams, D. (2022). eP198: EIF3F compound heterozygous genotype-phenotype association. Genetics in Medicine, 24(3), S123.

Lizzi, M. (2021). Investigation of the role of eukaryotic initiation factor 3f (eIF3f) and heterogeneous nuclear ribonucleoprotein K (hnRNP K) in stress induced RNA disruption in melanoma cells (Doctoral dissertation, Laurentian University of Sudbury).

Hüffmeier, U., Kraus, C., Reuter, M. S., Uebe, S., Abbott, M. A., Ahmed, S. A., ... & Zweier, C. (2021). EIF3F-related neurodevelopmental disorder: refining the phenotypic and expanding the molecular spectrum. Orphanet journal of rare diseases, 16(1), 1-9.

Andoh, T., Yoshihisa, Y., Rehman, M. U., Tabuchi, Y., & Shimizu, T. (2021). Berberine induces anti-atopic dermatitis effects through the downregulation of cutaneous EIF3F and MALT1 in NC/Nga mice with atopy-like dermatitis. Biochemical Pharmacology, 185, 114439.

Li, J., Yu, W., Ge, J., Zhang, J., Wang, Y., Wang, P., & Shi, G. (2020). Targeting eIF3f Suppresses the Growth of Prostate Cancer Cells by Inhibiting Akt Signaling. OncoTargets and therapy, 13, 3739.

Docquier, A., Pavlin, L., Raibon, A., Bertrand‐Gaday, C., Sar, C., Leibovitch, S., ... & Bernardi, H. (2019). eIF3f depletion impedes mouse embryonic development, reduces adult skeletal muscle mass and amplifies muscle loss during disuse. The Journal of Physiology, 597(12), 3107-3131.

ChaoHui, L., ZhenYu, Z., Ling, X., HuiLing, R., & XiaoJun, W. (2019). Interaction between influenza A virus NS1 protein and host protein eIF3f promotes viral replication. Zhongguo Yufang Shouyi Xuebao/Chinese Journal of Preventive Veterinary Medicine, 41(10), 999-1003.

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For research use only. Not intended for any clinical use.

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