For research use only.
| Verified Samples | Verified Samples in WB: Mouse brain Verified Samples in IHC: Mouse brain |
| Dilution | WB 1:1000-2000, IHC 1:100-200 |
| Isotype | IgG |
| Host | Mouse |
| Reactivity | Mouse |
| Applications | WB, IHC-p, IF |
| Clonality | Monoclonal |
| Immunogen | Recombinant Protein |
| Abbre | HIF-1 β/ARNT |
| Synonyms | ARNT, ARNT protein, Aryl hydrocarbon receptor nuclear translocator, Class E basic helix-loop-helix protein 2, Dioxin receptor, Dioxin receptor nuclear translocator, Drnt, HIF 1 beta, HIF 1beta, HIF-1-beta, HIF1-beta, HIF1B, HIF1beta, Hypoxia Inducible Fact, arnT, bHLHe2 |
| Swissprot | |
| Observed MW | 87 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 | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol. |
| Purification Method | Protein A purification |
| Research Areas | Cancer, Cardiovascular, Epigenetics and Nuclear Signaling, Metabolism |
| Clone No. | 4C5 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | Hypoxia-inducible factor 1 (HIF1) is a heterodimeric transcription factor that plays a critical role in the cellular response to hypoxia (1). The HIF1 complex consists of two subunits, HIF-1α and HIF-1β, which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family (2). HIF1 regulates the transcription of a broad range of genes that facilitate responses to the hypoxic environment, including genes regulating angiogenesis, erythropoiesis, cell cycle, metabolism and apoptosis. The widely expressed HIF-1α is typically degraded rapidly in normoxic cells by the ubiquitin/proteasomal pathway. Under normoxic conditions, HIF-1α is proline hydroxylated leading to a conformational change that promotes binding to the von Hippel Lindau protein (VLH) E3 ligase complex; ubiquitination and proteasomal degradation follows (3,4). Both hypoxic conditions and chemical hydroxylase inhibitors (such as desferrioxamine and cobalt) inhibit HIF-1α degradation and lead to its stabilization. In addition, HIF-1α can be induced in an oxygen-independent manner by various cytokines through the PI3K-AKT-mTOR pathway (5-7).HIF-1β is also known as AhR nuclear translocator (ARNT) due to its ability to partner with the aryl hydrocarbon receptor (AhR) to form a heterodimeric transcription factor complex (8). Together with AhR, HIF-1β plays an important role in xenobiotics metabolism (8). |
Other Clones
1 Results
Other Formats
1 Results
Unconjugated
