E-Cadherin Polyclonal Antibody (AN004540L)
For research use only.
| Verified Samples |
Verified Samples in WB: MCF-7 |
| Dilution | WB 1:250-1:500 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Human E-Cadherin protein expressed by E.coli |
| Abbre | E-Cadherin |
| Synonyms | Arc 1, Arc 1, CADH1, Cadherin 1, cadherin 1 type 1 E-cadherin, Cadherin1, CAM 120/80, CD 324, CD324, CD324 antigen, cdh1, CDHE, E-Cad/CTF3, E-cadherin, ECAD, Epithelial cadherin, epithelial calcium dependant adhesion protein, LCAM, Liver cell adhesion molecule, UVO, Uvomorulin, Arc-1, Cadherin 1, cadherin 1 type 1 E-cadherin, Cadherin1, CD 324, CD324 antigen, E-Cad/CTF3, epithelial calcium dependant adhesion protein, Liver cell adhesion molecule, CDH, Arc, CADH, CD antigen CD, Cleaved into: E-Cad/CTF, Cadherin, CAM 120/, Arc-1, CD324, CDHE, ECAD, LCAM, UVO, CDH1, E-Cadherin, CADH1, Cadherin-1, Uvomorulin, E-Cad, CTF2, CAM 120/80, Epithelial cadherin, CD antigen CD324, Cleaved into: E-Cad/CTF1, CTF3, CDH1 |
| Swissprot | |
| Calculated MW | 98 kDa |
| Observed MW |
120 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 | Cell membrane, Endosome, Golgi apparatus, Cytoplasm |
| Tissue Specificity | Expressed in granuloma macrophages (at protein level). Expressed in the liver. |
| 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 | Signal Transduction, Cancer, Developmental Biology, Tags & Cell Markers |
| 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 | Epithelial (E) - Cadherin (ECAD), also known as cell-CAM120/80 in the human, uvomorulin in the mouse, Arc-1 in the dog, and L-CAM in the chicken, is a member of the cadherin family of cell adhesion molecules. Cadherins are calcium-dependent transmembrane proteins, which bind to one another in a homophilic manner. On their cytoplasmic side, they associate with the three catenins, alpha, beta, and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Without association with the catenins, the cadherins are non-adhesive. Cadherins play a role in development, specifically in tissue formation. They may also help to maintain tissue architecture in the adult. E-Cadherin may also play a role in tumor development, as loss of E-Cadherin has been associated with tumor invasiveness. E-Cadherin is a classical cadherin molecule. Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating calcium‑dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. E‑Cadherin contains five extracellular calcium-binding domains of approximately 110 amino acids each. |
Other Clones
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Unconjugated
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