SDF-1α Rat Recombinant is a 7.9 kDa polypeptide chain comprising 68 amino acids, synthesized in Escherichia coli using proprietary chromatographic purification techniques . It is a non-glycosylated protein formulated as a sterile, lyophilized powder in phosphate buffer (pH 7.4) with 150 mM NaCl .
Gene: Encoded by the CXCL12 gene, located on chromosome 10 in rats. Alternative splicing produces six isoforms, with SDF-1α (CXCL12a) being the most prevalent .
Protein Structure:
Contains three conserved β-strands and an α-helix core, stabilized by disulfide bonds .
The disordered N-terminus (residues 1–8) mediates receptor (CXCR4) binding, while the C-terminus interacts with glycosaminoglycans (GAGs) for cellular anchoring .
Monomeric at nanomolar concentrations but dimerizes under specific conditions (e.g., phospholipid bicelles) .
Mechanism: SDF-1α binds CXCR4, activating intracellular pathways (e.g., Akt, ERK) to promote chemotaxis of hematopoietic stem cells (HSCs) and mesenchymal stem cells (BMSCs) .
Applications:
Ischemic Cardiomyopathy: SDF-1α reduces infarct size by 30% in rat models through stem cell homing and direct cardioprotection .
Pulmonary Hypertension: Downregulation of SDF-1α in the right ventricle correlates with disease progression .
Myocardial Infarction (MI): Adenoviral delivery of SDF-1α post-MI in rats improves left ventricular ejection fraction (LVEF) by 11% and reduces fibrosis .
Clinical Trials: Phase II trials (e.g., STOP-HF) show improved LVEF in severe heart failure patients treated with SDF-1α gene therapy .
SDF-1α is a small protein with a molecular weight of approximately 7.9 kDa, consisting of 68 amino acid residues . It is produced by stromal cells and functions primarily through its interaction with the CXCR4 receptor, a G-protein-coupled receptor. This interaction is essential for the chemotaxis of lymphocytes and macrophages, migration of hematopoietic cells from the fetal liver to the bone marrow, and the formation of large blood vessels .
Recombinant SDF-1α, such as the rat recombinant version, is produced using E. coli expression systems . This recombinant protein is used extensively in research to study its biological functions and potential therapeutic applications. It is highly purified, with a purity of ≥ 98% as determined by SDS-PAGE gel and HPLC analyses .