Ambient

Sonic Hedgehog (Shh) is a member of the Hedgehog (Hh) family of highly conserved proteins which are widely represented throughout the animal kingdom. In mammal, there are three related Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh). They share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). Sonic Hedgehog plays a role in cell growth, cell specialization, and the normal shaping (patterning) of the body. Shh is also important for development of the brain and spinal cord (central nervous system), eyes, limbs, and many other parts of the body.

Sonic Hedgehog (Shh) is a member of the Hedgehog (Hh) family of highly conserved proteins which are widely represented throughout the animal kingdom. In mammal, there are three related Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh). They share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). Sonic Hedgehog plays a role in cell growth, cell specialization, and the normal shaping (patterning) of the body. Shh is also important for development of the brain and spinal cord (central nervous system), eyes, limbs, and many other parts of the body.

Sonic Hedgehog (Shh) is a member of the Hedgehog (Hh) family of highly conserved proteins which are widely represented throughout the animal kingdom. In mammal, there are three related Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh). They share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). Sonic Hedgehog plays a role in cell growth, cell specialization, and the normal shaping (patterning) of the body. Shh is also important for development of the brain and spinal cord (central nervous system), eyes, limbs, and many other parts of the body.

Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems.

Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems.

Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems.

Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems.

Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems.

Shikimic Acid

Shikimic Acid

Shikimic Acid

Shikimic Acid

Shikimic Acid

Shikimic Acid

Shikimic Acid

Molecular Formula : C7 H10 O5

Molecular Formula : C7 H10 O5

Molecular Formula : C7 H10 O5

Molecular Formula : C9H14O5

Molecular Formula : C9H14O5

Molecular Formula : C9H14O5

Molecular Formula : C62H42O6Ru2

Molecular Formula : C62H42O6Ru2

Molecular Formula : C62H42O6Ru2

Molecular Formula : C32 H54 N2 O23

Molecular Formula : C32 H54 N2 O23

Molecular Formula : C13H19NOS • HCl

Molecular Formula : C13H19NOS • HCl

Molecular Formula : C13H19NOS • HCl

Molecular Formula : C17 2H6 H20 Cl N

Molecular Formula : C17 2H6 H20 Cl N

Molecular Formula : C17 H26 Cl N . Cl H . H2 O

Molecular Formula : C17 H26 Cl N . Cl H . H2 O

Molecular Formula : C17 H26 Cl N . Cl H . H2 O

Siglec-10 is immune system-restricted and highly expressed in peripheral blood leukocytes. Siglec-10 preferably binds to α-2,3- or α-2,6-linked sialic acid (similarity). Siglec10 is involved in the negative regulation of B cell antigen receptor signal transduction. The inhibition of B cell activation depends on PTPN6/SHP-1 (by similarity). The binding of Siglec10 to CD24 may be involved in the selective suppression of the immune response (by similarity) to risk-related molecular patterns (DAMPs) (such as HMGB1, HSP70 and HSP90). The combination of Siglec10 and CD24 may regulate the immune response of natural killer (NK) cells. Play a role in controlling autoimmunity (by similarity). In the process of initiating an adaptive immune response by CD8-α+ dendritic cells, cross-presentation is inhibited by weakening the formation of MHC class I peptide complexes. The function seems to imply the recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex, thereby promoting phagosome acidification (by similarity).

Siglec-10 is immune system-restricted and highly expressed in peripheral blood leukocytes. Siglec-10 preferably binds to α-2,3- or α-2,6-linked sialic acid (similarity). Siglec10 is involved in the negative regulation of B cell antigen receptor signal transduction. The inhibition of B cell activation depends on PTPN6/SHP-1 (by similarity). The binding of Siglec10 to CD24 may be involved in the selective suppression of the immune response (by similarity) to risk-related molecular patterns (DAMPs) (such as HMGB1, HSP70 and HSP90). The combination of Siglec10 and CD24 may regulate the immune response of natural killer (NK) cells. Play a role in controlling autoimmunity (by similarity). In the process of initiating an adaptive immune response by CD8-α+ dendritic cells, cross-presentation is inhibited by weakening the formation of MHC class I peptide complexes. The function seems to imply the recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex, thereby promoting phagosome acidification (by similarity).

Siglec-10 is immune system-restricted and highly expressed in peripheral blood leukocytes. Siglec-10 preferably binds to α-2,3- or α-2,6-linked sialic acid (similarity). Siglec10 is involved in the negative regulation of B cell antigen receptor signal transduction. The inhibition of B cell activation depends on PTPN6/SHP-1 (by similarity). The binding of Siglec10 to CD24 may be involved in the selective suppression of the immune response (by similarity) to risk-related molecular patterns (DAMPs) (such as HMGB1, HSP70 and HSP90). The combination of Siglec10 and CD24 may regulate the immune response of natural killer (NK) cells. Play a role in controlling autoimmunity (by similarity). In the process of initiating an adaptive immune response by CD8-α+ dendritic cells, cross-presentation is inhibited by weakening the formation of MHC class I peptide complexes. The function seems to imply the recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex, thereby promoting phagosome acidification (by similarity).

Siglec-15 preferentially recognizes the Neu5Acalpha2-6GalNAcalpha- structure. Siglec-15 associates with the activating adaptor proteins DNAX activation protein (DAP)12 and DAP10 via its lysine residue in the transmembrane domain. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike Siglec-14, however, it does not have an inhibitory counterpart.

Siglec-15 preferentially recognizes the Neu5Acalpha2-6GalNAcalpha- structure. Siglec-15 associates with the activating adaptor proteins DNAX activation protein (DAP)12 and DAP10 via its lysine residue in the transmembrane domain. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike Siglec-14, however, it does not have an inhibitory counterpart.

Siglec-15 preferentially recognizes the Neu5Acalpha2-6GalNAcalpha- structure. Siglec-15 associates with the activating adaptor proteins DNAX activation protein (DAP)12 and DAP10 via its lysine residue in the transmembrane domain. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike Siglec-14, however, it does not have an inhibitory counterpart.

CD22, or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins. It is found on the surface of mature B cells and to a lesser extent on some immature B cells. CD22 a member of the immunoglobulin superfamily. CD22 functions as an inhibitory receptor for B cell receptor (BCR) signaling. It is also involved in the B cell trafficking to Peyer’s patches in mice.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Molecular Formula : C6 H13 N O3 Si

Molecular Formula : C6 H13 N O3 Si

Molecular Formula : C22 H30 N6 O4 S

Molecular Formula : C22 H30 N6 O4 S