reliatech

Description: RELMα, also known as ‘found in inflammatory zone 1’ (FIZZ1) belongs to the RELM/FIZZ family of cysteine rich secretory proteins. RELMα is most abundantly expressed in white adipose tissue but not in pre-adipocytes or 3T3L1 adipocytes. RELMα expression is also detected in mammary tissue, heart, lung, and tongue.

Description: RELMα, also known as ‘found in inflammatory zone 1’ (FIZZ1) belongs to the RELM/FIZZ family of cysteine rich secretory proteins. RELMα is most abundantly expressed in white adipose tissue but not in pre-adipocytes or 3T3L1 adipocytes. RELMα expression is also detected in mammary tissue, heart, lung, and tongue.

Description: Relaxin-3 (H3 relaxin, Insulin-like peptide-7, INSL7) is a secreted protein structurally related to insulin, which is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as “somatostatin-like” or “angiotensin-like” peptide receptor, and also binds specifically to the LGR7 receptor, previously identified as an “orphan” G protein coupled receptor. Signaling by Relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of Relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Relaxin-3 is a 5.5 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.

Description: Human RELM beta is a 19.0 kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELM beta, 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 RELM beta is highly homologous to that of the adipose-derived cytokine Resistin and RELMa. 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 RELM beta is a 19.0 kDa homodimer consisting of two identical 89 amino acid chains linked by a single disulfide bond.

Description: Human RELM beta is a 19.0 kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELM beta, 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 RELM beta is highly homologous to that of the adipose-derived cytokine Resistin and RELMa. 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 RELM beta is a 19.0 kDa homodimer consisting of two identical 89 amino acid chains linked by a single disulfide bond.

Description: RELMβ (Resistin-like molecule β/FIZZ2) is an 18 kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMβ, 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 (Rajala, M. et al. J. Clin. Invest. Vol. 111, 225-230 (2003)). Interestingly the molecular structure of RELMβ is highly homologous to that of the adipose-derived cytokine Resistin and RELMβ. 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 RELMβ is an 18.0 kDa, consisting of two 83 amino acid residue chains.

Description: RELMβ (Resistin-like molecule β/FIZZ2) is an 18 kDa disulfide-linked homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMβ, 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 (Rajala, M. et al. J. Clin. Invest. Vol. 111, 225-230 (2003)). Interestingly the molecular structure of RELMβ is highly homologous to that of the adipose-derived cytokine Resistin and RELMβ. 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 RELMβ is an 18.0 kDa, consisting of two 83 amino acid residue chains.

Description: RELMα belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The other three known members of this family; Resistin, RELMα, and RELMβ, 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. RELMγ is most closely related to RELMα, but is distinctly secreted to bone marrow, spleen, lung, and in peripheral blood granulocytes. The physiological role of RELMγ may include the promotion or regulation of promyelocytic differentiation, although the specific molecular targets of RELMγ have not been identified. Recombinant murine RELMγ is a 9.2 kDa monomeric protein containing 88 amino acid residues.

Description: RELMα belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The other three known members of this family; Resistin, RELMα, and RELMβ, 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. RELMγ is most closely related to RELMα, but is distinctly secreted to bone marrow, spleen, lung, and in peripheral blood granulocytes. The physiological role of RELMγ may include the promotion or regulation of promyelocytic differentiation, although the specific molecular targets of RELMγ have not been identified. Recombinant murine RELMγ is a 9.2 kDa monomeric protein containing 88 amino acid residues.

Description: RELMα belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The three known members of this family; Resistin, RELMα and RELMβ 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. RELMα and Resistin are secreted exclusively by adipocytes while RELMβ is expressed in the epithelium of the colon and small bowel. The physiological role and molecular targets of RELMα re still unknown. Recombinant murine RELMα is a 10.0 kDa monomeric protein containing 88 amino acid residues.

Description: RELMα belongs to a unique family of tissue-specific cytokines termed FIZZ (found in inflammatory zone) and RELM. The three known members of this family; Resistin, RELMα and RELMβ 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. RELMα and Resistin are secreted exclusively by adipocytes while RELMβ is expressed in the epithelium of the colon and small bowel. The physiological role and molecular targets of RELMα re still unknown. Recombinant murine RELMα is a 10.0 kDa monomeric protein containing 88 amino acid residues.

Description: Relaxin-2 is a peptide hormone structurally related to insulin, which is expressed in the placenta, decidua, prostate, and in the ovary during pregnancy. Of the three known relaxin genes, Relaxin-2 is the only relaxin known to circulate in the blood. Relaxin-2 binds specifically to the LGR7 and LGR8 receptors, previously identified as an “orphan” G protein coupled receptors. Signaling by Relaxin-2 through its target receptors enhances the growth of pubic ligaments and ripening of the cervix during birth. Recombinant Relaxin-2 is a nonglycosylated 6.0 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 29 amino acid B-chain.

Description: Relaxin-2 is a peptide hormone structurally related to insulin, which is expressed in the placenta, decidua, prostate, and in the ovary during pregnancy. Of the three known relaxin genes, Relaxin-2 is the only relaxin known to circulate in the blood. Relaxin-2 binds specifically to the LGR7 and LGR8 receptors, previously identified as an “orphan” G protein coupled receptors. Signaling by Relaxin-2 through its target receptors enhances the growth of pubic ligaments and ripening of the cervix during birth. Recombinant Relaxin-2 is a nonglycosylated 6.0 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 29 amino acid B-chain.

Description: Relaxin-3 (H3 relaxin, Insulin-like peptide-7, INSL7) is a secreted protein structurally related to insulin, which is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as “somatostatin-like” or “angiotensin-like” peptide receptor, and also binds specifically to the LGR7 receptor, previously identified as an “orphan” G protein coupled receptor. Signaling by Relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of Relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Relaxin-3 is a 5.5 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.

Description: Relaxin-3 (H3 relaxin, Insulin-like peptide-7, INSL7) is a secreted protein structurally related to insulin, which is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as “somatostatin-like” or “angiotensin-like” peptide receptor, and also binds specifically to the LGR7 receptor, previously identified as an “orphan” G protein coupled receptor. Signaling by Relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of Relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Relaxin-3 is a 5.5 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.