Recombinant TIA1 Monoclonal Antibody (AN301676L)
For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, Jurkat, K562, MOLT-4, NIH-3T3 Verified Samples in FCM: Jurkat Verified Samples in IP: Jurkat cells extracts |
| Dilution | WB 1:500-1:2000, FCM 1:50-1:100, IP 1:50-1:100 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, FCM, IP |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human TIA1 fragment |
| Abbre | TIA1 |
| Synonyms | TIA, TIA1, TIA-1, WDM, Cytotoxic granule associated RNA binding protein, Cytotoxic granule associated RNA binding protein 1, mTIA-1, Nucleolysin TIA 1 isoform p40, Nucleolysin TIA1 isoform p40, Nucleolysin TIA-1 isoform p40, p40 TIA 1, p40-TIA-1, p40-TIA-1 (containing p15-TIA-1), RNA binding protein TIA 1, RNA binding protein TIA1, RNA-binding protein TIA-1, T-cell-restricted intracellular antigen-1, TIA 1, TIA 1 cytotoxic granule associated RNA binding protein, TIA1 cytotoxic granule associated RNA binding protein, TIA1 cytotoxic granule associated RNA binding protein like 1, TIA1 protein, TIAL1, TIAR |
| Swissprot | |
| Calculated MW | 43 kDa |
| Observed MW |
42-43 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 |
| 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, Epigenetics and Nuclear Signaling, Cancer |
| Clone No. | A379 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis. |
Other Clones
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Other Formats
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Unconjugated
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