Cytokines & Chemokines

Recombinant Rat IL-21 (Legacy Tebubio ref. 167400-41). IL‐21 is a pleiotropic cytokine produced by CD4+ T cells in response to antigenic stimulation. Its action generally enhances antigen‐specific responses of immune cells. The biological effects of IL‐21 include: inducing the differentiation of T cell‐stimulated B cells into plasma cells and memory B cells; the stimulation of IgG production in conjunction with IL‐4; and the induction of apoptotic effects in naïve B cells and stimulated B cells in the absence of T cell signaling. Additionally, IL‐21 promotes the anti‐tumor activity of CD8+ T cells and NK cells. IL‐21 exerts its effect through binding to a specific type I cytokine receptor, IL‐21R, which also contains the γ chain (γc) found in other cytokine receptors, including IL‐2, IL‐4, IL‐7, IL‐9 and IL‐15. The IL‐21/IL‐21R interaction triggers a cascade of events, which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors S

Recombinant Human Resistin (Legacy Tebubio ref. 167450-19). Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMalpha, RELMbeta, and RELMgamma, share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Human Resistin is a 19.5 kDa, disulfide-linked, homodimeric protein composed of two identical 92 amino acid chains lin

Recombinant Human Resistin (Legacy Tebubio ref. 167450-19). Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMalpha, RELMbeta, and RELMgamma, share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Human Resistin is a 19.5 kDa, disulfide-linked, homodimeric protein composed of two identical 92 amino acid chains lin

Recombinant Human RELMbeta (Legacy Tebubio ref. 167450-22). RELMbeta (Resistin-like molecule beta/FIZZ2) is a disulfide-linked, homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMbeta, and its molecular targets, are not fully known, but it has been suggested that it plays a regulatory role during inflammation, and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELMbeta is highly homologous to that of the adipose-derived cytokines, resistin and RELMalpha. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Recombinant Human RELMbeta is a 19.0 kDa protein, consisting of two identical 89 amino acid polypeptide chains linked by a single disulfide bond.

Recombinant Human RELMbeta (Legacy Tebubio ref. 167450-22). RELMbeta (Resistin-like molecule beta/FIZZ2) is a disulfide-linked, homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMbeta, and its molecular targets, are not fully known, but it has been suggested that it plays a regulatory role during inflammation, and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELMbeta is highly homologous to that of the adipose-derived cytokines, resistin and RELMalpha. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Recombinant Human RELMbeta is a 19.0 kDa protein, consisting of two identical 89 amino acid polypeptide chains linked by a single disulfide bond.

Recombinant Murine RELMalpha (Legacy Tebubio ref. 167450-26). RELMalpha belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The four known members of this family, resistin, RELMalpha, RELMbeta, and RELMgamma, are 85-94 amino acid, secreted proteins sharing a conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. RELMalpha and resistin are secreted exclusively by adipocytes, while RELMbeta is expressed in the epithelium of the colon and small bowel. The physiological role and molecular targets of RELMalpha are still unknown. Recombinant Murine RELMalpha is a 10.0 kDa monomeric protein containing 89 amino acid residues.

Recombinant Murine RELMalpha (Legacy Tebubio ref. 167450-26). RELMalpha belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The four known members of this family, resistin, RELMalpha, RELMbeta, and RELMgamma, are 85-94 amino acid, secreted proteins sharing a conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. RELMalpha and resistin are secreted exclusively by adipocytes, while RELMbeta is expressed in the epithelium of the colon and small bowel. The physiological role and molecular targets of RELMalpha are still unknown. Recombinant Murine RELMalpha is a 10.0 kDa monomeric protein containing 89 amino acid residues.

Recombinant Murine RELMbeta (Legacy Tebubio ref. 167450-26B). RELMbeta (Resistin-like molecule beta/FIZZ2) is a disulfide-linked, homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMbeta, and its molecular targets, are not fully known, but it has been suggested that it plays a regulatory role during inflammation, and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELMbeta is highly homologous to that of the adipose-derived cytokines, resistin and RELMalpha. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Recombinant Murine RELMbeta is an 18.0 kDa protein, consisting of two identical 83 amino acid polypeptide chains linked by a single disulfide bond.

Recombinant Murine RELMbeta (Legacy Tebubio ref. 167450-26B). RELMbeta (Resistin-like molecule beta/FIZZ2) is a disulfide-linked, homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMbeta, and its molecular targets, are not fully known, but it has been suggested that it plays a regulatory role during inflammation, and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELMbeta is highly homologous to that of the adipose-derived cytokines, resistin and RELMalpha. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Recombinant Murine RELMbeta is an 18.0 kDa protein, consisting of two identical 83 amino acid polypeptide chains linked by a single disulfide bond.