TrpE Antibody (17): sc-57607

TrpE Antibody (17) is a mouse monoclonal IgG1 kappa light chain antibody that detects TrpE protein of non-species reactive by western blotting (WB) and immunoprecipitation (IP). Anti-TrpE antibody (17) is available as a non-conjugated isotype antibody. TrpE protein, also known as anthranilate synthetase, plays a crucial role in the biosynthesis of the amino acid tryptophan, which is essential for protein synthesis and serves as a precursor for various bioactive compounds, including neurotransmitters and hormones. TrpE protein is located in the cytoplasm, where TrpE catalyzes the conversion of chorismate to anthranilate, a key step in the tryptophan biosynthetic pathway. TrpE regulation is vital, as TrpE is subject to feedback inhibition by tryptophan itself, ensuring that cellular levels of this amino acid remain balanced. TrpE′s ability to form insoluble constructs that are resistant to proteolysis allows for high-yield production, making TrpE a valuable marker in cellular studies. TrpE monoclonal antibody (17) is particularly advantageous as an immunoaffinity reagent, facilitating the purification and study of proteins in various research applications. Additionally, TrpE′s relevance in hydrophobic interaction chromatographic purification techniques underscores TrpE′s importance in both research and protein purification endeavors.

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TrpE Antibody (17) References:

1. Use of bacterial trpE fusion vectors to express and characterize the bovine immunodeficiency-like virus core protein.  |  Atkinson, B., et al. 1992. J Virol Methods. 36: 35-49. PMID: 1372612
2. A new series of trpE vectors that enable high expression of nonfusion proteins in bacteria.  |  Mercy, MR., et al. 1992. Protein Expr Purif. 3: 57-64. PMID: 1422208
3. Flavivirus type-specific antigens produced from fusions of a portion of the E protein gene with the Escherichia coli trpE gene.  |  Fonseca, BA., et al. 1991. Am J Trop Med Hyg. 44: 500-8. PMID: 1648310
4. Isolation of a monoclonal antibody to the TrpE protein and its use for the purification of recombinant fusion proteins.  |  Nurse, F., et al. 1991. Hybridoma. 10: 753-60. PMID: 1816074
5. Nucleotide sequence of trpE, anthranilate synthase I gene, of Bacillus caldotenax.  |  Shiratsuchi, A. and Sato, S. 1991. Biochim Biophys Acta. 1090: 348-50. PMID: 1840498
6. Protection conferred by TrpE fusion proteins containing portions of the C-terminal region of capsid protein VP1 of foot-and-mouth disease virus.  |  Giavedoni, LD., et al. 1991. J Gen Virol. 72 (Pt 4): 967-71. PMID: 1849980
7. The Rhizobium meliloti trpE(G) gene is regulated by attenuation, and its product, anthranilate synthase, is regulated by feedback inhibition.  |  Bae, YM. and Crawford, IP. 1990. J Bacteriol. 172: 3318-27. PMID: 2111807
8. Use of TrpE fusion protein to identify antigenic domains within the BIV envelope protein.  |  Chen, P., et al. 1994. J Virol Methods. 47: 331-43. PMID: 7520916
9. Purification of antisera against a trpE fusion protein by negative immunoabsorption.  |  Liu, ZX. and Bergold, PJ. 1994. Biotechniques. 16: 426-8. PMID: 8185916