(KO Validated) STAT3 Polyclonal Antibody (E-AB-62227)
- +1
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Verified Samples | Verified Samples in WB:HeLa, 293T Verified Samples in IF: Rat brain, Mouse brain |
Dilution | WB 1:500-1:2000, IF 1:50-1:200 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Applications | WB, IF |
Clonality | Polyclonal |
Immunogen | Recombinant fusion protein of human STAT3 (NP_644805.1). |
Abbre | STAT3 |
Synonyms | ADMIO, ADMIO1, APRF, HIES, STAT3, Stat3 |
Swissprot | |
Calculated MW | 83 kDa/87 kDa/88 kDa |
Observed MW | 90 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 | Cytoplasm. Nucleus. Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1. |
Concentration | 1 mg/mL |
Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
Purification Method | Affinity purification |
Research Areas | Cancer, Cardiovascular, Epigenetics and Nuclear Signaling, Developmental Biology, Signal Transduction, Stem Cells |
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 | The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. This protein is activated through phosphorylation in response to various cytokines and growth factors including IFNs, EGF, IL5, IL6, HGF, LIF and BMP2. This protein mediates the expression of a variety of genes in response to cell stimuli, and thus plays a key role in many cellular processes such as cell growth and apoptosis. The small GTPase Rac1 has been shown to bind and regulate the activity of this protein. PIAS3 protein is a specific inhibitor of this protein. Mutations in this gene are associated with infantile-onset multisystem autoimmune disease and hyper-immunoglobulin E syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms. |
Other Clones
1 Results
Other Formats
1 Results
Unconjugated
- Leptin Selectively Regulates Nutrients Metabolism in Nile Tilapia Fed on High Carbohydrate or High Fat Diet
IF:3.519
Journal:Frontiers in Endocrinology(2018)
DOI:10.3389/fendo.2018.00574Reactivity:Nile tilapia
Sample Type:Tissue homogenate