EEF1D Human
Description
EEF1D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 301 amino acids (1-281 a.a.) and having a molecular mass of 33.2kDa (Molecular weight on SDS-PAGE will appear higher). The EEF1D is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS LAGSSGPGAS SGTSGDHGEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I.
Product Science Overview
Eukaryotic Translation Elongation Factor 1 Delta (EEF1D) is a crucial component of the protein synthesis machinery in eukaryotic cells. It is part of the elongation factor-1 (EF-1) complex, which plays a significant role in the elongation phase of translation, where amino acids are added to the growing polypeptide chain.
EEF1D is a subunit of the EF-1 complex, which is responsible for the enzymatic delivery of aminoacyl-tRNAs to the ribosome. Specifically, EEF1D functions as a guanine nucleotide exchange factor (GEF). It stimulates the exchange of GDP bound to EF-1 alpha (another subunit of the EF-1 complex) to GTP, thereby regenerating EF-1 alpha for another round of aminoacyl-tRNA delivery to the ribosome .
EEF1D has been implicated in various diseases. For instance, it has been reported that following HIV-1 infection, EEF1D interacts with the HIV-1 Tat protein. This interaction results in the repression of translation of host cell proteins and enhanced translation of viral proteins . Additionally, autoantibodies against EEF1D have been identified in patients with autoimmune cerebellar ataxia, suggesting its potential role as a biomarker for early detection and diagnosis of this condition .
EEF1D is ubiquitously expressed in human tissues, reflecting its fundamental role in protein synthesis. It is also found to be frequently overexpressed in human cancer cells, indicating its potential involvement in tumorigenesis . The regulation of EEF1D expression and its activity is complex and involves multiple layers of control, including transcriptional, post-transcriptional, and post-translational modifications.
Human recombinant EEF1D is produced using recombinant DNA technology, which involves cloning the EEF1D gene into an expression vector, introducing the vector into a suitable host cell (such as E. coli or yeast), and then purifying the expressed protein. Recombinant EEF1D is used in various research applications, including studies on protein synthesis, translation regulation, and disease mechanisms.
