Recombinat Human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of Human Umbilical Vein Endothelial cells.
The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein contsists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus.
Result by N-terminal sequencing: SKLKD
Length: 661 amino acids.
mRNA RefSeq: NM_0001159920
Recombinat Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1D1-5) is a 72 kDa protein containing amino acid residues. The baculovirus generated, recombinant Human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70kDa.
Result by N-terminal sequencing: SGSKLKD
Recombinant human sIL-2R alpha is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2R alpha. Due to glycosylation, IL-2R alpha has an approximate molecular weight of 31 kDa based on SDS-PAGE gel and Mass Spectrometry.