Recombinant eIF3G Monoclonal Antibody (AN301973L)

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For research use only.
Verified Samples |
Verified Samples in WB: K562, 293T, NIH-3T3, PC-12 Verified Samples in IHC: Human colon cancer, Mouse cerebrum, Rat cerebrum Verified Samples in IF: 293T, K-562 Verified Samples in FCM: K-562 |
Dilution | WB 1:1000-1:2000, IHC 1:50-1:100, IF 1:50-1:100, FCM 1:50 |
Isotype | IgG, κ |
Host | Rabbit |
Reactivity | Human, Rat, Mouse |
Applications | WB, IHC, IF, FCM |
Clonality | Monoclonal;Recombinant |
Immunogen | Peptide. This information is proprietary to PTMab. |
Abbre | eIF3G |
Synonyms | EIF3S, EIF3G, EIF3-P42, EIF3S4, eIF3-delta, eIF3-p44 |
Swissprot | |
Calculated MW | 36 kDa |
Observed MW |
40 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
Cellular Localization | Nucleus, Cytoplasm |
Concentration | 1 mg/mL |
Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
Purification Method | Protein A purified |
Research Areas | Epigenetics and Nuclear Signaling |
Clone No. | A689 |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | Ice bag |
background | eIF3 is a large translation initiation complex with 10 to 13 different subunits. eIF3A, eIF3B, eIF3C, eIF3E, eIF3F, and eIF3H are the core subunits critical for the function of this complex. eIF3 physically interacts with eIF4G, which may be responsible for the association of the 40S ribosomal subunit with mRNA. eIF3 also stabilizes the binding of Met-tRNAf.eIF2.GTP to the 40S ribosomal subunit and helps keep the integrity of the resulting complex upon addition of the 60S ribosomal subunit. Studies have shown that mTOR interacts with eIF3 directly. When cells are stimulated by hormones or mitogenic signals, mTOR binds to the eIF3 complex and phosphorylates S6K1. This process results in the dissociation of S6K1 from eIF3 and S6K1 activation. The activated S6K1 then phosphorylates its downstream targets including ribosomal protein S6 and eIF4B, resulting in stimulation of translation. Further findings demonstrated that activated mTOR signaling induces the association of eIF3 with eIF4G upon stimulation with insulin. |
Other Clones
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Unconjugated
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