Recombinant TLS/FUS Monoclonal Antibody (AN301003L)
For research use only.
| Verified Samples |
Verified Samples in WB: HepG2 Verified Samples in IHC: Mouse brain tissue, Rat brain tissue |
| Dilution | IHC 1:500-1:2000, WB 1:500-1:2000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human TLS/FUS protein |
| Abbre | TLS |
| Synonyms | ETM, ALS, POMP, HNRNPP, FUS, ALS6, ETM4, FUS1, HNRNPP2, POMP75, TLS, RNA-binding protein FUS, ALS6, ETM4, FUS1, HNRNPP2, POMP75, RNA-binding protein FUS, TLS, 16) in malignant liposarcoma), 16) malignant liposarcoma, 75 kDa DNA pairing protein, 75 kDa DNA-pairing protein, Amyotrophic lateral sclerosis 6, FUS CHOP, Fus like protein, Fused in sarcoma, Fusion (involved in t(12, Fusion derived from t(12, Fusion gene in myxoid liposarcoma, Heterogeneous nuclear ribonucleoprotein P2, hnRNP P2, Oncogene FUS, Oncogene TLS, RNA binding protein FUS, TLS CHOP, Translocated in liposarcoma, Translocated in liposarcoma protein |
| Swissprot | |
| Calculated MW | 53 kDa |
| Observed MW |
70 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 | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Epigenetics and Nuclear Signaling, Cancer |
| Clone No. | 12B9 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The hnRNP complex is involved in pre-mRNA splicing and the export of fully processed mRNA to the cytoplasm. This protein belongs to the FET family of RNA-binding proteins which have been implicated in cellular processes that include regulation of gene expression, maintenance of genomic integrity and mRNA/microRNA processing. Alternative splicing results in multiple transcript variants. Defects in this gene result in amyotrophic lateral sclerosis type 6. |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
-
IF：{{item.impact}}
Journal：{{item.journal}} ({{item.year}})
DOI：{{item.doi}}Reactivity：{{item.species}}
Sample Type：{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
