CDH1 Human, Sf9

E-Cadherin Human Recombinant, Sf9
Cat. No.
BT27611
Source
Sf9, Baculovirus cells.
Synonyms
Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CDH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 694 amino acids (24-709a.a.) and having a molecular mass of 76.6kDa. 
(Molecular size on SDS-PAGE will appear at approximately 70kDa).
CDH1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
E-cadherin, also known as uvomorulin or cell-CAM120/80, is a calcium-dependent cell adhesion molecule primarily found in epithelial tissues. It plays a crucial role in cellular growth and development by regulating tissue architecture and maintaining tissue integrity. Extensive research has shown a strong correlation between decreased or absent E-cadherin expression in carcinomas and their increased likelihood of invasion and metastasis.
Description
CDH1, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 694 amino acids (24-709a.a.) with a molecular mass of 76.6 kDa. Note that on SDS-PAGE, the molecular size will appear around 70 kDa. This CDH1 protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
The CDH1 protein solution is provided at a concentration of 0.5 mg/ml and contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, freeze the product at -20°C. Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the CDH1 protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
EPEPCHPGFD AESYTFTVPR RHLERGRVLG RVNFEDCTGR QRTAYFSLDT RFKVGTDGVI TVKRPLRFHN PQIHFLVYAW DSTYRKFSTK VTLNTVGHHH RPPPHQASVS GIQAELLTFP NSSPGLRRQK RDWVIPPISC PENEKGPFPK NLVQIKSNKD KEGKVFYSIT GQGADTPPVG VFIIERETGW LKVTEPLDRE RIATYTLFSH AVSSNGNAVE DPMEILITVT DQNDNKPEFT QEVFKGSVME GALPGTSVME VTATDADDDV NTYNAAIAYT ILSQDPELPD KNMFTINRNT GVISVVTTGL DRESFPTYTL VVQAADLQGE GLSTTATAVI TVTDTNDNPP IFNPTTYKGQ VPENEANVVI TTLKVTDADA PNTPAWEAVY TILNDDGGQF VVTTNPVNND GILKTAKGLD FEAKQQYILH VAVTNVVPFE VSLTTSTATV TVDVLDVNEA PIFVPPEKRV EVSEDFGVGQ EITSYTAQEP DTFMEQKITY RIWRDTANWL EINPDTGAIS TRAELDREDF EHVKNSTYTA LIIATDNGSP VATGTGTLLL ILSDVNDNAP IPEPRTIFFC ERNPKPQVIN IIDADLPPNT SPFTAELTHG ASANWTIQYN DPTQESIILK PKMALEVGDY KINLKLMDNQ NKDQVTTLEV SVCDCEGAAG VCRKAQPVEA GLQIPALEHH HHHH.

Product Science Overview

Structure and Function

E-Cadherin is a single-pass transmembrane protein composed of several distinct regions:

  • Extracellular Domain: This domain consists of five tandemly repeated subdomains, each containing conserved regions that serve as calcium-binding sites . The extracellular domain forms X-shaped cis dimers within one cell, and these dimers interact with adjacent cells to form trans dimers, creating a “zipper” structure that facilitates cell-cell adhesion .
  • Intracellular Domain: The intracellular domain is highly phosphorylated and is vital for binding to β-catenin . β-catenin, in turn, binds to α-catenin, which links the cadherin complex to the actin cytoskeleton, providing structural stability .
Recombinant Production in Sf9 Cells

Sf9 cells, derived from the fall armyworm (Spodoptera frugiperda), are commonly used for the production of recombinant proteins, including E-Cadherin . The recombinant production process involves the following steps:

  1. Gene Cloning: The gene encoding human E-Cadherin is cloned into a suitable expression vector.
  2. Transfection: The expression vector is introduced into Sf9 cells using a method such as baculovirus-mediated transfection.
  3. Protein Expression: The transfected Sf9 cells are cultured under conditions that promote the expression of the recombinant E-Cadherin protein.
  4. Protein Purification: The expressed protein is purified using techniques such as affinity chromatography to obtain a high-purity product .
Applications and Importance

Recombinant E-Cadherin produced in Sf9 cells is used in various research and clinical applications, including:

  • Cancer Research: E-Cadherin is a key player in epithelial-mesenchymal transition (EMT), a process implicated in cancer metastasis. Studying E-Cadherin can provide insights into cancer progression and potential therapeutic targets .
  • Cell Adhesion Studies: E-Cadherin is essential for understanding the mechanisms of cell-cell adhesion and the role of adherens junctions in tissue integrity .
  • Drug Development: Recombinant E-Cadherin can be used in drug screening assays to identify compounds that modulate its function, potentially leading to new treatments for diseases involving cell adhesion defects .

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