[The production and characteristics of polyclonal antibodies to the threonine-containing site of the cytoplasmic domain of the EGF receptor]. Tsitologiia 1993;35(4):68-72
Date
01/01/1993Pubmed ID
8328026Scopus ID
2-s2.0-0027350161 (requires institutional sign-in at Scopus site) 1 CitationAbstract
A conjugate of a synthetic polypeptide to hemocyanine was used as an antigen for obtaining polyclonal antibodies to the site of cytoplasmic domain of the epidermal growth factor (EGF) receptor. The amino acid sequence of the peptide used was the same as that of the EGF receptor from residue 650 to 661. In the A431 cell solubilizate the obtained antibodies interact with the phosphorylated protein with 170 kDa molecular weight (MW), by immunoblotting recognize the protein of this MW, and as evidenced by immunofluorescence, their distribution in the cell is the same as that of monoclonal antibodies to the EGF receptor. It is concluded that the obtained antibodies may recognize the EGF receptor. Moreover, these antibodies in solubilizates of A431, CHO cells, and normal human fibroblasts by immunoblotting recognize 74 and 76 kDa proteins.
Author List
Sorokin AB, Aleksandrov KE, Vinogradova NA, Nesterov AM, Nikol'skiĭ NNAuthor
Andrey Sorokin PhD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Antibodies
Cells, Cultured
Cricetinae
Cytoplasm
ErbB Receptors
Fluorescent Antibody Technique
Humans
Immunization
Immunoblotting
Molecular Sequence Data
Molecular Weight
Precipitin Tests
Rabbits
Threonine
