HSP90 alpha Polyclonal Antibody (E-AB-70141)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela, HepG2, MCF-7, Human colon cancer, Mouse colon, Mouse brain, Rat brain |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | KLH conjugated Synthetic peptide corresponding to Mouse HSP90A |
| Abbre | HSP90 alpha |
| Synonyms | EL52, Heat shock 86 kDa, Heat shock 90kD protein 1, Heat shock 90kDa protein 1 alpha, Heat shock protein 90kDa alpha (cytosolic) class A , alpha, alpha like 4, alpha-like 4, epididymis luminal secretory protein 52, heat shock 90kD protein, heat shock 90kD protein 1 |
| Swissprot | |
| Calculated MW | 90 kDa |
| Observed MW |
90 kDa
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, Cytoplasm, Membrane, Nucleus. |
| Concentration | 460 μg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 1% protein protectant and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cancer, Signal Transduction |
| 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 | HSP90,encoded by HSP90AA1,is a constitutively and ubiquitously expressed molecular chaperone that is crucial for the stability and function of many proteins. HSP90 provides chaperoning activity for client proteins; many of them are members of oncogenic pathways,indicating its implication in tumor malignancy. HSP90 mainly resides in the cytosol,while it can also be released to the extracellular space. Secreted Hsp90 is a C-terminal truncated form. It has been reported that the level of plasma Hsp90 is positively correlated with tumor malignancy in clinical cancer patients,and can be a promising diagnostic marker for tumor malignancy in clinical application. |
Other Clones
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Unconjugated
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