Recombinant TNF receptor II Monoclonal Antibody (AN301888L)
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For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, Jurkat, Raji Verified Samples in IHC: Human breast cancer, Mouse liver Verified Samples in IF: Jurkat |
| Dilution | WB 1:500-1:1000, IHC 1:50-1:100, IF 1:50 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, IHC, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human TNF receptor II fragment |
| Abbre | TNF receptor II |
| Synonyms | soluble TNFR1B variant, Tumor necrosis factor receptor, tumor necrosis factor binding protein, CD120b, TBPII, TNF-R-II, TNF-R75, TNFBR, TNFR1B, TNFR2, TNFR80, p75, p75TNFR, TNF Receptor II, TNFRSF1B, p80 TNF-alpha receptor, Tumor Necrosis Factor Receptor II, Etanercept, P75tbpii, TNF-R2, TNFR2TNFR1B, TNFRII, TNF-RII, TNFR-II, CD120b antigen, p75 TNF receptor, soluble TNFR1B variant 1, TNF RII, TNFBRp80 TNF-alpha receptor, tumor necrosis factor beta receptor, tumor necrosis factor binding protein 2, Tumor necrosis factor receptor 2, tumor necrosis factor receptor superfamily member 1B, tumor necrosis factor receptor superfamily, member 1B, Tumor necrosis factor receptor type II, p80, Tumor Necrosis Factor Receptor II |
| Swissprot | |
| Calculated MW | 48 kDa |
| Observed MW |
63 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 | Cell membrane, Secreted |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Cell Biology, Immunology, Signal Transduction, Cancer, Cardiovascular, Neuroscience |
| Clone No. | A604 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | TNF receptor II (TNF-R2) is one of the receptors of TNF-α. The two receptors for TNF-α, TNF-R1 (55 kDa) and TNF-R2 (75 kDa), can mediate distinct cellular responses. In most cases, cytotoxicity elicited by TNF has been reported to act through TNF-R1. In contrast, TNF-R2 appears to be important in T cell signaling and responses to infection. TNF-R2 binds to distinct members of the TRAF family, leading to the activation of NF-κB. Soluble forms of both receptors have also been characterized which can bind TNF-α and may play an important role in immune disorders. |
Other Clones
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