Vimentin Polyclonal Antibody (AN005800L)
For research use only.
| Verified Samples | Verified Samples in WB: U-2 OS, 293 |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Human Vimentin protein expressed by E.coli |
| Abbre | Vimentin |
| Synonyms | CTRCT30, HEL113, vimentin, CTRCT30, Epididymis luminal protein 113, FLJ36605, HEL113, VIM, VIME, Vimentin, HEL, Epididymis luminal protein, CTRCT, CTRCT30, HEL113, Vimentin, VIM, Epididymis luminal protein 113, VIME, FLJ36605, epididymis secretory sperm binding protein |
| Swissprot | |
| Calculated MW | 54 kDa |
| Observed MW |
57 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 matrix, Cell membrane |
| Tissue Specificity | Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines. |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Research Areas | Neuroscience, Signal Transduction, Stem Cells, Cancer, Developmental Biology |
| 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 | Vimentin is a type III intermediate filament (IF) protein found in various non-epithelial cells, especially mesenchymal cells. A vimentin monomer, has a central α-helical domain and carboxyl (tail) domains. Two monomers compose the basic subunit of vimentin assembly. Vimentin is crucial for supporting and anchoring the position of the organelles in the cytosol. Vimentin provided cells with a resilience absent from the microtubule or actin filament networks, when under mechanical stress in vivo. Therefore, in general, it is accepted that vimentin is the cytoskeletal component responsible for maintaining cell integrity. Vimentin is also responsible for stabilizing cytoskeletal interactions. It is found that vimentin control the transport of low-density lipoprotein. It has been used as a sarcoma tumor marker to identify mesenchyme. |
Other Clones
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Unconjugated
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