| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Large proline-rich protein BAG6; BAG family molecular chaperone regulator 6; BCL2-associated athanogene 6; BAG-6; HLA-B-associated transcript 3; Protein G3; Protein Scythe; BAG6; BAT3 |
| Cellular Localization | |
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| Host | |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of human EIF4EBP1, which shares 75% and 81.2% amino acid (aa) sequence identity with mouse and rat EIF4EBP1, respectively. |
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| UniProt # |
Overview
Anti-EIF4EBP1 Antibody Picoband® is an antibody for EIF4EBP1 detection raised in Rabbit (Polyclonal, Rabbit IgG), with reported reactivity: Human,Mouse,Rat. Commonly used in WB, IHC, Flow Cytometry, ELISA workflows.
Key elements and design rationale
- Target: EIF4EBP1 (BCL2 associated athanogene 6); UniProt: Q13541
- Antibody format: Rabbit, Polyclonal, Rabbit IgG
- Molecular weight: 17 kDa
- Applications: WB, IHC, Flow Cytometry, ELISA
Vendor description (summary): Boster Bio Anti-EIF4EBP1 Antibody Picoband® catalog # A00968-1.
Biological background
Biological context: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate to the production of antigenic peptides and play a role in antigen presentation in immune response (By similarity). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, inly regulates the insulin-like growth factor receptor signaling pathway. Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2) Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC).
Expression and localization notes: cellular localization: Cytosol, Nucleus, exosome., tissue context: Expressed by immature dendritic cells..
Common research applications
- Western blotting (WB): Compare EIF4EBP1 levels across samples and conditions using appropriate loading and biological controls.
- Immunohistochemistry (IHC): Evaluate spatial distribution of EIF4EBP1 in tissue sections, considering fixation and antigen retrieval effects.
- Flow cytometry: Quantify EIF4EBP1-positive populations in single-cell suspensions with appropriate gating and controls.
- ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.
Notes for experimental interpretation
- Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
- Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.
Additional product notes (from provided fields)
- Background: Eukaryotic translation initiation factor 4E-binding protein 1 (also known as 4E-BP1) is a protein that in humans is encoded by the EIF4EBP1 gene. This gene encodes one member of a family of translation repressor proteins. The protein ly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation.
- Cross reactivity: No cross-reactivity with other proteins.
- Cellular localization: Cytosol, Nucleus, exosome.
- Tissue details: Expressed by immature dendritic cells.
- Research category: Adapters,Cytokines,Immunology,Innate Immunity,Interleukins,Macrophage/Inflammation,Signal Transduction,Transmembrane
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.