Cytokines & Chemokines

Recombinant Human Leptin (Legacy Tebubio ref. 167300-27). Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant Human Leptin is a 16.0 kDa protein containing 147 amino acid residues.

Recombinant Human Leptin (Legacy Tebubio ref. 167300-27). Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant Human Leptin is a 16.0 kDa protein containing 147 amino acid residues.

Recombinant Human Leptin Receptor (Legacy Tebubio ref. 167300-27R). Encoded for, along with leptin, by the obese (ob) gene, leptin receptor is a single-transmembrane-domain protein of the Type I, or Class I, Cytokine Receptor Family. The full length isoform, OB-Rb, is highly expressed in hypothalamic neurons, T cells, and the vascular endometrium, and is thought to be the only isoform capable of transducing intracellular signals. Isoform OB-Ra, which is widely distributed at varying levels of expression, demonstrates weak signal activity and has been implicated in the active transport of leptin across the blood-brain barrier. Through ligand-binding with leptin receptor and the subsequent JAK2/STAT3 signaling cascade, the adipose-derived cytokine leptin functions to suppress appetite and increase thermogenesis. Leptin and leptin receptor have also, more recently, been implicated in the regulation of immune function, reproduction, glucose homeostasis, bone metabolism, wound healing, hema

Recombinant Human Leptin Receptor (Legacy Tebubio ref. 167300-27R). Encoded for, along with leptin, by the obese (ob) gene, leptin receptor is a single-transmembrane-domain protein of the Type I, or Class I, Cytokine Receptor Family. The full length isoform, OB-Rb, is highly expressed in hypothalamic neurons, T cells, and the vascular endometrium, and is thought to be the only isoform capable of transducing intracellular signals. Isoform OB-Ra, which is widely distributed at varying levels of expression, demonstrates weak signal activity and has been implicated in the active transport of leptin across the blood-brain barrier. Through ligand-binding with leptin receptor and the subsequent JAK2/STAT3 signaling cascade, the adipose-derived cytokine leptin functions to suppress appetite and increase thermogenesis. Leptin and leptin receptor have also, more recently, been implicated in the regulation of immune function, reproduction, glucose homeostasis, bone metabolism, wound healing, hema

Recombinant Human SDF-1alpha (CXCL12) (Legacy Tebubio ref. 167300-28A). SDF-1alpha and beta are stromal-derived, CXC chemokines that signal through the CXCR4 receptor. SDF-1alpha and beta chemoattract B and T cells, and have been shown to induce migration of CD34+ stem cells. Additionally, the SDF-1 proteins exert HIV-suppressive activity in cells expressing the CXCR4 receptor. Human and murine SDF-1 proteins act across species. SDF-1alpha and beta contain the four highly conserved cysteine residues present in CXC chemokines. The mature SDF-1alpha protein is the result of alternative splicing of the SDF-1 gene and contains 68 amino acid residues. Recombinant Human SDF-1alpha is an 8.0 kDa protein containing 68 amino acid residues.

Recombinant Human SDF-1alpha (CXCL12) (Legacy Tebubio ref. 167300-28A). SDF-1alpha and beta are stromal-derived, CXC chemokines that signal through the CXCR4 receptor. SDF-1alpha and beta chemoattract B and T cells, and have been shown to induce migration of CD34+ stem cells. Additionally, the SDF-1 proteins exert HIV-suppressive activity in cells expressing the CXCR4 receptor. Human and murine SDF-1 proteins act across species. SDF-1alpha and beta contain the four highly conserved cysteine residues present in CXC chemokines. The mature SDF-1alpha protein is the result of alternative splicing of the SDF-1 gene and contains 68 amino acid residues. Recombinant Human SDF-1alpha is an 8.0 kDa protein containing 68 amino acid residues.

Recombinant Human SDF-1beta (CXCL12) (Legacy Tebubio ref. 167300-28B). SDF-1alpha and beta are stromal-derived, CXC chemokines that signal through the CXCR4 receptor. SDF-1alpha and beta chemoattract B and T cells, and have been shown to induce migration of CD34+ stem cells. Additionally, the SDF-1 proteins exert HIV-suppressive activity in cells expressing the CXCR4 receptor. Human and murine SDF-1 proteins act across species. SDF-1alpha and beta contain the four highly conserved cysteine residues present in CXC chemokines. The mature SDF-1beta protein, produced by an N-terminal truncation of two additional amino acids, after removal of the signal sequence, contains 72 amino acid residues. Recombinant Human SDF-1beta is an 8.5 kDa protein containing 72 amino acid residues.

Recombinant Human SDF-1beta (CXCL12) (Legacy Tebubio ref. 167300-28B). SDF-1alpha and beta are stromal-derived, CXC chemokines that signal through the CXCR4 receptor. SDF-1alpha and beta chemoattract B and T cells, and have been shown to induce migration of CD34+ stem cells. Additionally, the SDF-1 proteins exert HIV-suppressive activity in cells expressing the CXCR4 receptor. Human and murine SDF-1 proteins act across species. SDF-1alpha and beta contain the four highly conserved cysteine residues present in CXC chemokines. The mature SDF-1beta protein, produced by an N-terminal truncation of two additional amino acids, after removal of the signal sequence, contains 72 amino acid residues. Recombinant Human SDF-1beta is an 8.5 kDa protein containing 72 amino acid residues.

Recombinant Human SDF-1gamma (CXCL12) (Legacy Tebubio ref. 167300-28G). The SDF‐1 proteins are stromal‐derived CXC chemokines that signal primarily through the CXCR4 receptor. SDF‐1 proteins exert chemotactic activity over a broad range of immune system cell types and may also be involved in other processes including metastasis of certain cancers, inflammation, and angiogenesis. Additionally, SDF‐1 can suppress HIV entry into cells expressing the CXCR4 receptor. Five isomers of SDF‐1 have been found with SDF‐1alpha being the predominant form, expressing in a wide range of cell types. The SDF‐1gamma isoform is distinctive in that it contains a highly basic C‐terminal region, which presumably is the reason for its high binding affinity to gylcosaminoglycans (GAG) and heparin sulfate (HS). Consequently, most of SDF‐1gamma exists in a cell‐ and membrane‐bound form, which confers greater stability compared to other isoforms via increased resistance to proteolytic degradation. SDF‐1gamma bin