GenScript Nanjing Inc.

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.

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.

Signal regulatory protein alpha (SIRPα, designated CD172a), is also known as CD172 antigen-like family member A (CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), which is a monomeric about 90kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily. SIRPα is Ubiquitous and highly expressed in brain. SIRPA/CD172a is immunoglobulin-like cell surface receptor for CD47 and acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPA/SHPS-1 supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment and may play a key role in intracellular signaling during synaptogenesis and in synaptic function by similarity. SIRPα recognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production.

Signal regulatory protein alpha (SIRPα, designated CD172a), is also known as CD172 antigen-like family member A (CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), which is a monomeric about 90kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily. SIRPα is Ubiquitous and highly expressed in brain. SIRPA/CD172a is immunoglobulin-like cell surface receptor for CD47 and acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPA/SHPS-1 supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment and may play a key role in intracellular signaling during synaptogenesis and in synaptic function by similarity. SIRPα recognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production.

Surfactant protein D is a member of the collectin family of innate immune modulators. It is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures, that contains a N-terminal collagen-like domain and a C-terminal lectin domain that are characteristic of members of the collectin family of proteins, and also shows calcium-dependent binding to specific saccharides. Besides it is involved in the development of acute and chronic inflammation of the lung. Several human lung diseases are characterized by decreased levels of bronchoalveolar SP-D.

SPARC, an acronym for ’secreted protein, acidic and rich in cysteine’, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid , 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

SPARC, an acronym for ’secreted protein, acidic and rich in cysteine’, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid , 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

Staphylokinase (SAK), a 16kDa profibrinolytic protein from the Staphylococcus aureus, has been demonstrated to induce highly fibrin-specific thrombolysis in both human plasma and in limited clinical trials. Recent studies on the thrombolytic potential of recombinant SAK in achieving early perfusion in myocardial infarction and in the dissolution of platelet-rich clot have clearly established its immense utility in clinical medicine as a thrombolytic agent and suggested that it can be developed as a potent clot-dissolving agent.

Staphylokinase (SAK), a 16kDa profibrinolytic protein from the Staphylococcus aureus, has been demonstrated to induce highly fibrin-specific thrombolysis in both human plasma and in limited clinical trials. Recent studies on the thrombolytic potential of recombinant SAK in achieving early perfusion in myocardial infarction and in the dissolution of platelet-rich clot have clearly established its immense utility in clinical medicine as a thrombolytic agent and suggested that it can be developed as a potent clot-dissolving agent.

Streptavidin is a biotin-binding protein found in the culture broth of the bacterium Streptomyces avidinii. Streptavidin can bind to four moles of biotin per mole of protein,and it shows extremely high affinity, approximately 10,000-15,000 Da. Streptavidin lacks the carbohydrate side chains present on avidin and has an isoelectric point of 6.5 to avidin’s 10 far closer to that at which most useful biological interactions occur. As a result, Streptavidin frequently exhibits much lower non-specific binding than avidin does.