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Mouse Anti-EIF3D Recombinant Antibody (CBFYE-0676) (CBMAB-E1096-FY)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBFYE-0676
Antibody Isotype
IgG1, κ
Application
ELISA, IF, IP, WB

Basic Information

Immunogen
Amino acids 1-300 mapping at the N-terminus of human eIF3ζ.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
ELISA1:100-1:1,000
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500

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

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Eukaryotic Translation Initiation Factor 3 Subunit D
Introduction
Eukaryotic translation initiation factor-3 (eIF3), the largest of the eIFs, is a multiprotein complex composed of at least ten nonidentical subunits. The complex binds to the 40S ribosome and helps maintain the 40S and 60S ribosomal subunits in a dissociated state. It is also thought to play a role in the formation of the 40S initiation complex by interacting with the ternary complex of eIF2/GTP/methionyl-tRNA, and by promoting mRNA binding. The protein encoded by this gene is the major RNA binding subunit of the eIF3 complex.
Entrez Gene ID
8664
UniProt ID
O15371
Alternative Names
Eukaryotic Translation Initiation Factor 3 Subunit D; Eukaryotic Translation Initiation Factor 3, Subunit 7 Zeta, 66/67kDa; EIF3 P66; EIF3S7; Eukaryotic Translation Initiation Factor 3, Subunit D; Eukaryotic Translation Initiation Factor 3 Subunit 7
Research Area
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (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:18599441, PubMed:25849773).

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).

In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815).

(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).
Biological Process
Cap-dependent translational initiation Source: UniProtKB
Formation of cytoplasmic translation initiation complex Source: UniProtKB-UniRule
IRES-dependent viral translational initiation Source: UniProtKB
Positive regulation of mRNA binding Source: ParkinsonsUK-UCL
Positive regulation of translation Source: ParkinsonsUK-UCL
Translational initiation Source: UniProtKB
Viral translational termination-reinitiation Source: UniProtKB
Cellular Location
Cytoplasm
Involvement in disease
Defects in EIF3D are associated with some cancers, such as prostate, breast and colon cancers. Disease susceptibility may be associated with variants affecting the gene represented in this entry. Down-regulation inhibits proliferation of cancers (PubMed:25370813, PubMed:25322666, PubMed:25682860, PubMed:26617750, PubMed:26008152, PubMed:26036682, PubMed:27035563).
More Infomation

Thompson, L., Depledge, D. P., Burgess, H. M., & Mohr, I. (2022). An eIF3d-dependent switch regulates HCMV replication by remodeling the infected cell translation landscape to mimic chronic ER stress. Cell Reports, 39(5), 110767.

Li, X., Wang, Z., Liu, G., & Guo, J. (2021). EIF3D promotes the progression of preeclampsia by inhibiting of MAPK/ERK1/2 pathway. Reproductive Toxicology, 105, 166-174.

Balaban, S., Beduk, T., Durmus, C., Aydindogan, E., Salama, K. N., & Timur, S. (2021). Laser‐scribed Graphene Electrodes as an Electrochemical Immunosensing Platform for Cancer Biomarker ‘eIF3d’. Electroanalysis, 33(4), 1072-1080.

Lamper, A. M., Fleming, R. H., Ladd, K. M., & Lee, A. S. (2020). A phosphorylation-regulated eIF3d translation switch mediates cellular adaptation to metabolic stress. Science, 370(6518), 853-856.

Herrmannová, A., Prilepskaja, T., Wagner, S., Šikrová, D., Zeman, J., Poncová, K., & Valášek, L. S. (2020). Adapted formaldehyde gradient cross-linking protocol implicates human eIF3d and eIF3c, k and l subunits in the 43S and 48S pre-initiation complex assembly, respectively. Nucleic acids research, 48(4), 1969-1984.

Huang, H., Gao, Y., Liu, A., Yang, X., Huang, F., Xu, L., ... & Chen, L. (2019). EIF3D promotes sunitinib resistance of renal cell carcinoma by interacting with GRP78 and inhibiting its degradation. EBioMedicine, 49, 189-201.

Wang, D., Jia, Y., Zheng, W., Li, C., & Cui, W. (2019). Overexpression of eIF3D in lung adenocarcinoma is a new independent prognostic marker of poor survival. Disease markers, 2019.

Maekawa, M., Hiyoshi, H., Nakayama, J., Kido, K., Sawasaki, T., Semba, K., ... & Higashiyama, S. (2019). Cullin-3/KCTD10 complex is essential for K27-polyubiquitination of EIF3D in human hepatocellular carcinoma HepG2 cells. Biochemical and Biophysical Research Communications, 516(4), 1116-1122.

Liu, G. Z., Liu, J. Z., Li, X. Q., Zhang, L., Li, S. J., Xiao, T. W., ... & Liu, Y. (2018). Knockdown of eukaryotic translation initiation factor 3 subunit D (eIF3D) inhibits proliferation of acute myeloid leukemia cells. Molecular and cellular biochemistry, 438(1), 191-198.

Szostak, E., García-Beyaert, M., Guitart, T., Graindorge, A., Coll, O., & Gebauer, F. (2018). Hrp48 and eIF3d contribute to msl-2 mRNA translational repression. Nucleic acids research, 46(8), 4099-4113.

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

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