BATF 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 145 amino acids (1-125 a.a.) and having a molecular mass of 16.2kDa. The BATF is purified by proprietary chromatographic techniques.
MGSSHHHHHH SSGLVPRGSH MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS PRFQP.
The Basic Leucine Zipper (bZIP) transcription factors are a large family of proteins found in all eukaryotes. These proteins play crucial roles in regulating gene expression by binding to specific DNA sequences. The bZIP domain is characterized by a region rich in basic amino acids, such as arginine and lysine, which facilitates DNA binding, and a leucine zipper motif that enables dimerization .
The bZIP domain consists of two main parts:
bZIP transcription factors are involved in various cellular processes, including:
Recombinant bZIP proteins are produced using genetic engineering techniques to study their function and potential therapeutic applications. These proteins are expressed in host cells, such as bacteria or yeast, and then purified for research purposes. Recombinant bZIP proteins are valuable tools for understanding the molecular mechanisms of gene regulation and for developing new treatments for diseases related to bZIP dysfunction .
Malfunctions in bZIP transcription factors are associated with various diseases, including cancer. For instance, aberrant expression of JUN and other bZIP proteins can lead to uncontrolled cell growth and tumorigenesis . Understanding the regulatory networks of bZIP transcription factors is essential for developing targeted therapies for these conditions.