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Catalog Number: (10366-780)
Supplier: Bioss
Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].


Catalog Number: (10468-872)
Supplier: Bioss
Description: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility.


Catalog Number: (10468-870)
Supplier: Bioss
Description: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility.


Catalog Number: (10366-770)
Supplier: Bioss
Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].


Catalog Number: (76083-798)
Supplier: Bioss
Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene.


Catalog Number: (10366-774)
Supplier: Bioss
Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].


Catalog Number: (76083-796)
Supplier: Bioss
Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene.


Catalog Number: (10366-776)
Supplier: Bioss
Description: Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate(GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].


Catalog Number: (10665-056)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (76109-616)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (10665-130)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (10665-058)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (76109-022)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (10665-060)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (10665-044)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


Catalog Number: (10665-126)
Supplier: Bioss
Description: The G protein-coupled receptor TGR5 is a 330-amino acid protein that is almost universally expressed in human tissues including heart, skeletal muscle, spleen, kidney, liver, small intestine, placenta, and leukocytes, but not in brain, colon (without mucosa), thymus, or lung. TGR5 is sensitive to bile acids and responds through a significant mechanism that coordinates energy homeostasis. Bile acids activate mitogen-activated protein (MAP) kinase pathways, specifically induce TGR5 internalization, promote an increase of guanosine 5'-O-3-thio-triphosphate binding in membrane fractions, and cause rapid intracellular cAMP production. Bile acids also provoke TGR5 to suppress macrophage functions. TGR5-controlled signaling pathways may be good candidates for drug targets to treat common metabolic diseases, such as obesity, type II diabetes, hyperlipidemia, and atherosclerosis.


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