Supplier: ProSci Inc.

Macrophage Inflammatory Protein 1 alpha and MIP1 beta, two closely related but distinct proteins, were originally co-purified from medium conditioned by a LPS-stimulated murine macrophage cell line. Mature mouse MIP1 alpha shares approximately 77% and 70% amino acid identity with human MIP1 alpha and mouse MIP1 beta, respectively. MIP1 proteins are expressed primarily in T cells, B cells, and monocytes after antigen or mitogen stimulation.

Supplier: ProSci Inc.

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: ProSci Inc.

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localises to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilises microtubules duing myotube formation. It is a cytoplasmic protein the localises to the Z-lines in skeletal muscles, while MuRF2 localises to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerisation motif boxes, in their central regions.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

Protein Kinase c alpha (PKC alpha) is an 77 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol, phosphatidylserine and phorbol esters) of the PKC family of serine/ threonine kinases that are involved in a wide range of physiological processes including mitogenesis, cell survival and transcriptional regulation. PKC alpha is an ubiquitously expressed PKC isozyme that has been implicated in the regulation of a broad range of cellular functions including proliferation, differentiation, development, migration, cell cell adhesion, cell extracellular matrix adhesion, and solute transport. The activation loop threonine (threonine 497 in PKC alpha) of conventional PKCs is phosphorylated by phosphoinositide dependent kinase 1 (PDK1). This phosphorylation is necessary for the autophosphorylation of threonine 638 in the carboxy terminus of PKC alpha, a step that is critical for regulating the rate of PKC alpha dephosphorylation and inactivation.

Supplier: Bioss

MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.