Overview

Description

  • Nature

    Recombinant
  • Source

    HEK 293 cells
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Sequence

      ASRRQKRDWV IPPISCPENE KGPFPKNLVQ IKSNKDKEGK VFYSITGQGA DTPPVGVFII ERETGWLKVT EPLDRERIAT YTLFSHAVSS NGNAVEDPME ILITVTDQND NKPEFTQEVF KGSVMEGALP GTSVMEVTAT DADDDVNTYN AAIAYTILSQ DPELPDKNMF TINRNTGVIS VVTTGLDRES FPTYTLVVQA ADLQGEGLST TATAVITVTD TNDNPPIFNP TTYKGQVPEN EANVVITTLK VTDADAPNTP AWEAVYTILN DDGGQFVVTT NPVNNDGILK TAKGLDFEAK QQYILHVAVT NVVPFEVSLT TSTATVTVDV LDVNEAPIFV PPEKRVEVSE DFGVGQEITS YTAQEPDTFM EQKITYRIWR DTANWLEINP DTGAISTRAE LDREDFEHVK NSTYTALIIA TDNGSPVATG TGTLLLILSD VNDNAPIPEP RTIFFCERNP KPQVINIIDA DLPPNTSPFT AELTHGASAN WTIQYNDPTQ ESIILKPKMA LEVGDYKINL KLMDNQNKDQ VTTLEVSVCD CEGAAGVCRK AQPVEAGL KL HHHHHHHHH
    • Molecular weight

      63 kDa including tags
    • Amino acids

      150 to 705
    • Tags

      His tag C-Terminus
    • Additional sequence information

      N-terminal linker (2 extra AA), C terminal linker (2 AA) and C-terminal His-tag (10 AA).

Specifications

Our Abpromise guarantee covers the use of ab216213 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Mass Spectrometry

    SDS-PAGE

  • Endotoxin level

    < 0.100 Eu/µg
  • Mass spectrometry

    LC-MS/MS
  • Purity

    > 95 % Densitometry.
    Purifed using Ni-NTA chromatography.
  • Form

    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -80°C.

    Constituents: 5% Trehalose, 96% PBS

  • Reconstitution
    Add 200 µL of deionized water to prepare a working stock solution of approximately 0.5 mg/mL. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

General Info

  • Alternative names

    • Arc 1
    • CADH1_HUMAN
    • Cadherin 1
    • cadherin 1 type 1 E-cadherin
    • Cadherin-1
    • 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
    see all
  • Function

    Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.
    E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.
  • Tissue specificity

    Non-neural epithelial tissues.
  • Involvement in disease

    Defects in CDH1 are the cause of hereditary diffuse gastric cancer (HDGC) [MIM:137215]. An autosomal dominant cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Note=Heterozygous germline mutations CDH1 are responsible for familial cases of diffuse gastric cancer. Somatic mutations in the has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer.
    Defects in CDH1 are a cause of susceptibility to endometrial cancer (ENDMC) [MIM:608089].
    Defects in CDH1 are a cause of susceptibility to ovarian cancer (OC) [MIM:167000]. Ovarian cancer common malignancy originating from ovarian tissue. Although many histologic types of ovarian neoplasms have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
  • Sequence similarities

    Contains 5 cadherin domains.
  • Post-translational
    modifications

    During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm. The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway. Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions.
  • Cellular localization

    Cell junction. Cell membrane. Endosome. Golgi apparatus > trans-Golgi network. Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane.
  • Information by UniProt

Images

  • 10% SDS-PAGE analysis of ab216213:

    Lane 1. M.W. marker - 21, 31, 45, 66, 97 kDa

    Lane 2. Reduced and boiled sample, 2.5 µg/lane

    Lane 3. Non-reduced and non-boiled sample, 2.5 µg/lane

References

ab216213 has not yet been referenced specifically in any publications.

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