Recombinant eIF4G1 Monoclonal Antibody (AN301953L)
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For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, PANC-1, C2C12 Verified Samples in IHC: Human breast cancer, Human lung adenocarcinoma, Human placenta |
| Dilution | WB 1:1000, IHC 1:500-1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human eIF4G1 fragment |
| Abbre | eIF4G1 |
| Synonyms | PARK, DKFZp686A, eIF 4 gamma, eIF-4-gamma, Eukaryotic translation initiation factor 4 gamma, IF4G, EIF4G1, EIF-4G1, EIF4F, EIF4G, EIF4GI, P220, PARK18, DKFZp686A1451, eIF 4 gamma 1, eIF 4G 1, eIF 4G1, EIF4 gamma, eIF-4G 1, eIF-4-gamma 1, Eukaryotic translation initiation factor 4 gamma 1, IF4G1 |
| Swissprot | |
| Calculated MW | 175 kDa |
| Observed MW |
250 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 | Stress granule |
| 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. | A669 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure. The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure. eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex. Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation. The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress. |
Other Clones
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