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SP1 and SP3 are ubiquitously expressed CACC-box binding proteins, which are dominant in ES cell nuclear extracts.
Plant lectins are carbohydrate binding proteins which are reported to be toxic to several plant pathogens [ 38].
The biological function of IGF peptides are also modulated by a family of IGF binding proteins, which are found in the circulation and in the extracellular fluids.
The ligand binding domain is considered to have evolved from prokaryotic periplasmic binding proteins which are involved in amino acid and nutrient transport in bacteria [ 26].
These two cellular proteins are small DNA binding proteins, which are able to modify DNA structure at the site of integration and increase the probability of integration.
Specificity protein 1 (SP1) belongs to a family of universally expressed zinc-finger DNA binding proteins, which are involved in transcriptional regulation of a variety of genes.
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Early phase was associated with dramatic up-regulation of structural and metal binding proteins, which were repressed in later phases.
The second group was comprised of the genes of G protein (Transducin, GTP binding protein) and AMP-binding (Adenosine monophosphate binding) protein, which are involved in signal perception and transduction.
Alba family proteins are small, basic, dimeric nucleic acid-binding proteins, which are widely distributed in archaea and a number of eukaryotes.
Photoaffinity labeling has been used as a promising approach to detection and isolation of carbohydrate-binding proteins, which are typically characterized by low binding affinity and selectivity.
This sequence may identify a larger family of low molecular mass GTP-binding proteins which are isoprenylated.
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