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Recombinant E-Cadherin/CDH1/E-cad/CD324 Monoclonal Antibody (AN300024P)

All Size Price Qty
100μL $ 380.00
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For research use only.

Verified Samples Verified Samples in WB: MCF7, A431
Dilution WB 1:500-1:2000,  IP 4-8 μL/mg of lysate
Isotype IgG
Host Rabbit
Reactivity Human
Applications WB,  IP
Clonality Rabbit Monoclonal
Immunogen Recombinant Human E-Cadherin / CDH1 / E-cad / CD324 Protein
Abbre CDH1
Synonyms 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,  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
Swissprot
Calculated MW 97 kDa
Observed MW 130 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 0.2 μm filtered solution in PBS
Purification Method Protein A
Research Areas Signal Transduction,  Cancer,  Developmental Biology,  Tags & Cell Markers
Clone No. 6C9
Conjugation Unconjugated
Storage This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Shipping Ice bag
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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