skeletal muscle

Muscle, skeletal receptor tyrosine-protein kinase, also known as Muscle-specific tyrosine-protein kinase receptor, Muscle-specific kinase receptor, and MUSK, is a single-pass type I membrane protein that belongs to the protein kinase superfamily and tyr protein kinase family. MUSK contains one FZ (frizzled) domain, three Ig-like C2-type (immunoglobulin-like) domains, and one protein kinase domain. This protein is a muscle-specific tyrosine kinase receptor and it may play a role in clustering of the acetylcholine receptor in the postsynaptic neuromuscular junction. MUSK expression is increased in muscle cells stimulated with Wnt or at conditions when the Wnt signaling was activated. MUSK is a muscle-specific receptor tyrosine kinase that is activated by agrin. It has a critical role in neuromuscular synapse formation. MUSK is a receptor tyrosine kinase that is a key mediator of agrin's action and is involved in neuromuscular junction (NMJ) organization. Defects in the MUSK encoding gene are a cause of autosomal recessive congenital myasthenic syndrome (CMS). Congenital myasthenic syndromes are inherited disorders of neuromuscular transmission that stem from mutations in presynaptic, synaptic, or postsynaptic proteins. MUSK mutations lead to decreased agrin-dependent AChR aggregation, a critical step in the formation of the neuromuscular junction. Mutations in this receptor encoding gene also have been associated with the congenital myasthenic syndrome.

Muscle contraction. Myosin-1 Protein, Bovine, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 30.9 kDa and the accession number is Q9BE40.

May have an involvement in muscle development or hypertrophy. FHL1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 40.3 kDa and the accession number is Q13642.

Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role. MYBPC2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 49.5 kDa and the accession number is Q14324.

Appears to have a function in striated muscle development and regeneration.

Appears to have a function in striated muscle development and regeneration. ENO3 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 54.3 kDa and the accession number is P21550.

MUSK Protein, Mouse, Recombinant (His & Myc & SUMO) is expressed in E. coli.

Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TNNI1 Protein, Mouse, Recombinant (Flag & His & Myc) is expressed in E. coli expression system with N-10xHis-Flag and C-Myc tag. The predicted molecular weight is 29.6 kDa and the accession number is Q9WUZ5.

Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TnTf Protein, Bovine, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 39.0 kDa and the accession number is Q8MKI3.

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. ACTA1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 45.8 kDa and the accession number is P68133.

MUSK Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 53.8 kDa and the accession number is O15146.

Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. TNNI2 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.2 kDa and the accession number is P13412.

Calsequestrin-1 is an isoform of calsequestrin. Calsequestrin is a calcium-binding protein of the sarcoplasmic reticulum. It helps hold calcium in the cisterna of the sarcoplasmic reticulum after a muscle contraction, even though the concentration of calcium in the sarcoplasmic reticulum is much higher than in the cytosol. Two forms of calsequestrin have been identified: Calsequestrin-2 and Calsequestrin-1. Calsequestrin-1 is found in fast skeletal muscle. The release of calsequestrin-bound calcium (through a calcium release channel) triggers muscle contraction. The active protein is not highly structured, more than 5% of it adopting a random coil conformation. When calcium binds there is a structural change whereby the alpha-helical content of the protein increases from 3 to 11%. Both forms of calsequestrin are phosphorylated by casein kinase 2, but the cardiac form is phosphorylated more rapidly and to a higher degree. Calsequestrin-1 is also secreted in the gut where it deprives bacteria of calcium ions.

Alpha-Parvin (PARVA) is a member of the Parvin family. PARVA contains two CH (calponin-homology) domains. PARVA is widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. PARVA interacts with integrin-linked protein kinase and probably with actin and the LD1 and LD4 motifs of PXN. PARVA may play a role in the regulation of cell adhesion and cytoskeleton organization. PARVA is also involved in ciliogenesis.

Cyclin-Dependent Kinase Inhibitor 1B (CDKN1B) is a Kinesin-related motor protein necessary for mitotic spindle assembly and chromosome segregation. CDKN1B is expressed in all tissues with highest levels observed in skeletal muscle. CDKN1B is a potent inhibitor of Cyclin E- and Cyclin A-CDK2 complexes. CDKN1B forms a complex with Cyclin Type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. In addition, CDKN1B acts as an inhibitor or an activator of Cyclin Type D-CDK4 complexes depending on its phosphorylation state and stoichometry.

Coronin 6, a newly identified member of the coronin family, is highly enriched at adult NMJs and regulates AChR clustering via modulating the interaction between receptors and the actin cytoskeletal network. Coronins are a family of conserved actin-binding proteins originally identified in the actin-rich structure of the amoeba Dictyostelium discoideum . To date, seven members of coronins have been identified in mammals, and most exhibit tissue-specific distribution patterns. Coronin 6 is prominently expressed in adult muscle and enriched at the NMJ. Studies with cultured myotubes reveal that Coronin 6 regulates both agrin- and laminin-induced AChR clustering and is important for anchoring AChRs onto the actin cytoskeleton. Also, both the C-terminal region and a conserved Arg29 residue at the N terminus of Coronin 6 are essential for its actin-binding activity and stabilization of AChR–cytoskeleton linkage. Importantly, in vivo knockdown of Coronin 6 in mouse skeletal muscle fibers leads to destabilization of AChR clusters, which demonstrates that Coronin 6 is a critical regulator of AChR clustering at the postsynaptic region of the NMJs through modulating the receptor-anchored actin cytoskeleton. The human Coronin 6 has five isoforms produced by alternative splicing, and tissue-specific expression of these isoforms are unclear.

Hyaluronidase-1 (HYAL1) is a secreted lysosomal hyaluronidase that belongs to the glycosyl hydrolase 56 family. HYAL1 contains one EGF-like domain and is highly expressed in the liver, kidney, and heart, but it is weakly expressed in the lung, placenta, and skeletal muscle. HYAL1 is thought to be involved in cell proliferation, migration, and differentiation. It may play a role in promoting tumor progression and blocking the TGFB1-enhanced cell growth. Mutations in HYAL1 are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency.

Serine protease inhibitor A3N(Serpin A3N) is a serine protease inhibitor that is structurally related to α1 antichymotrypsin encoded by the SERPINA3 gene. Serpin A3N is highly expressed in brain, testis, lung, thymus, and spleen. It is expressed with low levels in bone marrow, kidney and skeletal muscle. Serpin A3N secreted by Sertoli cells may regulate the activity of locally produced Granzyme B. Granzyme B inhibition by Serpin A3N may therefore regulate Granzyme Bmediated killing by cytotoxic lymphocytes, providing a means to disable cellmediated immune responses.

Phosphomannomutase 1 (PMM1) blongs to the eukaryotic PMM family. Phosphomannomutase 1 can catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose which required for a number of critical mannosyl transfer reactions. PMM1 is highly expressed in liver, heart, brain, and pancreas, but lower expression in skeletal muscle. In addition, PMM1 may be responsible for the degradation of glucose-1,6 bisphosphate in ischemic brain.

Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors. ADAM12 Protein, Mouse, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 58.4 kDa and the accession number is Q61824.

The very low density lipoprotein receptor, known as VLDLR, is a single-pass type 1 integral membrance protein and a member of the LDL receptor family. This receptor family includes LDL receptor, LRP, megalin, VLDLR and ApoER2, and is characterized by a cluster of cysteine-rich class A repeats, epidermal growth factor (EGF)-like repeats, YWTD repeats and an O-linked sugar sdomain. VLDLR contains 3 EGF-like domains, 8 LDL-receptor class A domains, as well as 6 LDL-receptor class B repeats, and is abundant in heart, skeletal muscle, also ovary and kidney, but not in liver. VLDLR binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. VLDLR mediates the phosphorylation of mDab1 (mammalian disabled protein) via binding to Reelin, and induces the modulation of Tau phosphorylation. This pathway regulates the migration of neurons along with the radial glial fiber network during brain development. Defects of VLDLR may be the cause of VLDLR-associated cerebellar hypoplasia (VLDLRCH), a syndrome characterized by moderate-to-profound mental retardation, delayed ambulation, and predominantly truncal ataxia.

Fibroblast growth factor receptor-like 1 (FGFRL1) also known as Fibroblast growth factor receptor 5 (FGFR5), is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A unique feature of FGFRL1/FGFR5 is that it does not contain an intracellular tyrosine kinase domain. Some muscle types, including the muscles of the tongue and the diaphragm, express FGFRL1/FGFR5 at relatively high level. In contrast, the heart and the skeletal muscles of the limbs, as well as many other organs (brain, lung, liver, kidney, gut) express Fgfrl1 only at basal level. It is conceivable that FGFRL1/FGFR5 interacts with other Fgfrs, which are expressed in cartilage and muscle, to modulate FGF signaling.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

SIRT1 belongs to the sirtuin family. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. SIRT1 is included in class I of the sirtuin family. It is a NAD-dependent protein deacetylase, which regulates processes such as apoptosis and muscle differentiation by deacetylating key proteins. It deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce proapoptotic program and modulate cell senescence. SIRT1 also deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. It is involved in HES1- and HEY2-mediated transcriptional repression. SIRT1 inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. It may serve as a sensor of the cytosolic ratio of NAD(+)/NADH, which is essential in skeletal muscle cell differentiation. It also deacetylates 'Lys-16' of histone H4 (in vitro). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus.

S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A14, also known as S100 calciumbinding protein A14, S114 and S100A14, is a cytoplasm protein which belongs to the S-100 family. It is expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.

Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells. Uracil-DNA glycosylase exists in two forms: mitochondrial uracil-DNA glycosylase 1 (UNG1) and nuclear uracil-DNA glycosylase 2 (UNG2). uracil-DNA glycosylase. This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2. The UNG2 term was used as a previous symbol for the CCNO gene (GeneID 10309), which has been confused with this gene, in the literature and some databases. Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5). A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.

Death domain-containing protein CRADD, also known as Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CRADD and RAIDD, is a protein which is constitutively expressed in most tissues, with particularly high expression in adult heart, testis, liver, skeletal muscle, fetal liver and kidney. CRADD / RAIDD contains oneCARD domain and onedeath domain. CRADD / RAIDD contains a death domain involved in the binding of RIP protein. The CARD domain mediates the interaction with caspase-2. FADD / MORT1 is a death domain (DD)-containing adaptor / signaling molecule that interacts with the intracellular DD of FAS / APO-I ( CD95 ) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 ( Mch5 / MACH / FLICE). CRADD / RAIDD has a dual-domain structure similar to that of FADD. CRADD / RAIDD has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD / RAIDD could play a role in regulating apoptosis in mammalian cells. CRADD / RAIDD is a apoptotic adaptor molecule specific for caspase-2 and FASL / TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD / RAIDD recruits caspase-2 to the TNFR-1 signalling complex.

Calumenin belongs to the CREC family. It contains 6 EF-hand domains. Calumenin is expressed in skeletal muscle (at protein level). Calumenin interacts with GGCX and RYR1 in the presence of calcium ions, but not in the presence of EDTA. Calumenin is Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. It seems to inhibit gamma-carboxylase GGCX. Calumenin also binds 7 calcium ions with a low affinity and may modulate calcium release from the sarcoplasmic reticulum.

LC3A, also known as MAP1LC3A, is one of the light chain subunits that function together with both MAP1A and/or MAP1B. MAP1A and MAP1B are microtubule-associated proteins that mediate the physical interactions between microtubules and components of the cytoskeleton. MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. As a light chain subunit, MAP1LC3A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP1LC3A is expressed as two alternatively spliced isoforms that are expressed in testis, brain, heart, liver, and skeletal muscle but are absent in thymus and peripheral blood leukocytes.

RUVBL1, also known as RVB1, is a component of the NuA4 histone acetyltransferase complex and belongs to the RuvB family. RUVBL1 is ubiquitously expressed with high expression in heart, skeletal muscle and testis. It possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity. RUVBL1 is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. RUVBL1 plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. It also is essential for cell proliferation. RUVBL1 may be able to bind plasminogen at cell surface and enhance plasminogen activation.

MAP1LC3B (Microtubule Associated Protein 1 Light Chain 3 beta, also known as LC3B) is a Protein Coding gene. The product of this gene is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. LC3B is a member of the MAP1 LC3 family. It is most abundantly expressed in the heart, brain, skeletal muscle, and testis. LC3B is a subunit of the neuronal microtubule and functions in the formation of autophagosomal vacuoles (autophagosomes). It is associated with MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. LC3B also plays a role in autophagy, a process that involves the bulk degradation of the cytoplasmic component.

Profilin 2, also known as PFN2, is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is highly expressed in brain, skeletal muscle and kidney and less strongly in heart, placenta, lung and liver. Profilin 2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. Profilin 2 is thought to regulate actin polymerization in response to extracellular signals. It inhibits the formation of IP3 and DG by binding to PIP2.

Fn14 (tumor necrosis factor receptor superfamily, member 12A), also known as TNFRSF12A, is the receptor for TNFSF12/TWEAK. Fn14 shares 82% amino acid identity with the mouse sequence. It contains a signal peptide, an extracellular domain, a membrane-anchoring domain, and a cytoplasmic domain. In response to FGF1, calf serum, or phorbol ester stimulation of human quiescent fibroblasts in vitro, the level of Fn14 is increased. A 1.2-kb FN14 transcript was expressed at high levels in heart, placenta, and kidney, at intermediate levels in lung, skeletal muscle, and pancreas, and at low levels in brain and liver. Also, elevated FN14 expression was found in human liver cancer cell lines and hepatocellular carcinoma specimens. Expression of mouse Fn14 was upregulated in hepatocellular carcinoma nodules that develop in 2 different transgenic mouse models of hepatocarcinogenesis. TNFRSF12A is the weak inducer of apoptosis in some cell types. It promotes angiogenesis and the proliferation of endothelial cells. TNFRSF12A may modulate cellular adhesion to matrix proteins.

PHYH belongs to the family of iron(II)-dependent oxygenases, which typically incorporate one atom of dioxygen into the substrate and one atom into the succinate carboxylate group. PHYH is expressed in liver, kidney, and T-cells, but not in spleen, brain, heart, lung and skeletal muscle. It converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. Defects in PHYH can cause Refsum disease (RD). RD is an autosomal recessive disorder characterized clinically by a tetrad of abnormalities: retinitis pigmentosa, peripheral neuropathy, cerebellar ataxia, and elevated protein levels in the cerebrospinal fluid (CSF). Patients exhibit accumulation of the branched-chain fatty acid, phytanic acid, in blood and tissues.

Serine/threonine-protein kinase TAO3, also known as cutaneous T-cell lymphoma-associated antigen HD-CL-9, CTCL-associated antigen HD-CL-9, Dendritic cell-derived protein kinase, JNK / SAPK-inhibitory kinase, Jun kinase-inhibitory kinase, Kinase from chicken homolog A, Thousand and one amino acid protein 3, JIK, TAOK3 and MAP3K18, is cytoplasm and peripheral membrane protein which belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and STE2 subfamily. Protein kinases are pivotal regulators of cell signaling that modulate each other's functions and activities through site-specific phosphorylation events. TAOK3 / JIK contains one protein kinase domain. TAOK3 / JIK is ubiquitously expressed at a low level, and highly expressed in peripheral blood leukocytes (PBLs), thymus, spleen, kidney, skeletal muscle, heart and liver. TAOK3 / JIK inhibits the basal activity of Jun kinase. It is negatively regulated by epidermal growth factor (EGF). When overexpressed, TAOK3 / JIK may activate ERK1 / ERK2 and JNK / SAPK.

Pyruvate dehydrogenase kinase 4 (PDK4) is a mitochondrial protein that regulates the TCA cycle.PDK4, a vital mitochondrial protein, controls the switch between glycolysis and oxidative phosphorylation based upon nutrient availability.Pyruvate dehydrogenase kinase 4 (PDK4) mRNA has been reported as an up-regulated gene in the heart and skeletal muscle of carnitine-deficient juvenile visceral steatosis (JVS) mice under fed conditions. PDK4 plays an important role in the inhibition of glucose oxidation via the phosphorylation of pyruvate dehydrogenase complex (PDC).PDK4 gene expression is stimulated by thyroid hormone (T(3)), glucocorticoids, and long chain fatty acids.

Serine / threonine-protein kinase SRPK3, also known as Muscle-specific serine kinase 1, Serine/arginine-rich protein-specific kinase 3, SR-protein-specific kinase 3, Serine / threonine-protein kinase 23, MSSK-1, SRPK3 and MSSK1, is a member of the protein kinase superfamily and CMGC Ser / Thr protein kinase family. SRPK3 is a protein kinase belonging to serine/arginine protein kinases (SRPK) family, which phosphorylates serine / arginine repeat-containing proteins, and is controlled by a muscle-specific enhancer directly regulated by MEF2. SRPK3 / MSSK1 contains one protein kinase domain. SRPK3 / MSSK1 is exclusively expressed in skeletal and heart muscle. It is required for normal muscle development. Myocyte enhancer factor 2 (MEF2) plays essential roles in transcriptional control of muscle development. Normal muscle growth and homeostasis require MEF2-dependent signaling by SRPK3.

Cyclin-Dependent Kinase 4 Inhibitor C (CDKN2C) is a member of the INK4 family of cyclin dependent kinase inhibitors. CDKN2C contains 4 ANK repeats and interacts with CDK4 or CDK6. Highest levels of CDKN2C can be found in skeletal muscle, pancreas, and heart. CDKN2C inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB and prevent the activation of the CDK kinases. Studies have been shown the roles of CDKN2C gene in regulating spermatogenesis, as well as in suppressing tumorigenesis.

Desmin is a cytoplasmic protein and belongs to the intermediate filament family. interacts with DST and MTM1. Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms. Desmin is the main intermediate filament in mature skeletal, cardiac and smooth-muscle cells. DES founctions as homopolymers to form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. .Defects in DES are cause of the myopathy myofibrillar type 1, cardiomyopathy dilated type 1I, and neurogenic scapuloperoneal syndrome Kaeser type.

Platelet Glycoprotein 4 (CD36) is an integral membrane glycoprotein that has multiple physiological functions. It is broadly expressed on a variety of cell types including microvascular endothelium, adipocytes, skeletal muscle, epithelial cells of the retina, breast, and intestine, smooth muscle cells, erythroid precursors, platelets, megakaryocytes, dendritic cells, monocytes/macrophages, and microglia. As a member of the scavenger receptor family, CD36 is a multiligand pattern recognition receptor that interacts with a large number of structurally dissimilar ligands, including long chain fatty acid (LCFA), advanced glycation end products (AGE), thrombospondin-1,oxidized lowdensity lipoproteins (oxLDLs), high density lipoprotein (HDL), phosphatidylserine, apoptotic cells, β amyloid fibrils (fAβ), collagens I and IV, and Plasmodium falciparuminfected erythrocytes. CD36 is required for the antiangiogenic effects of thrombospondin-1 in the corneal neovascularization assay. It plays a role in lipid metabolism and has been identified as a fatty acid translocase necessary for the binding and transport of LCFA in cells and tissues.

Acidic Fibroblast Growth Factor Intracellular-Binding Protein (FIBP) is highly expressed in the heart, skeletal muscle, and pancreas. Acidic Fibroblast Growth Factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FIBP is an intracellular protein that binds selectively to acidic fibroblast growth factor (aFGF). It is postulated that FIBP may be involved in the mitogenic action of aFGF.

Chloride Intracellular Channel Protein 2 (CLIC2) is a critical component of all living cells; it regulatescellular traffic of Chloride ion and it can be inserted into membranes anf form chloride ion channels. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions, channel activity depends on the pH. CLIC2 is involved in regulating membrane potential and organic solute transport. CLIC2 modulates the activity of RYR2 and inhibits Calcium influx. CLIC2 can be detected in the adult brain, liver, lung, heart, stomach, spleen and testis. It is expressed in fetal liver and adult skeletal muscle. CLIC2 is a potential candidate for one of many diseases linked to Xq28.

The Interleukin-17 family proteins, comprising six members (IL-17, IL-17B through IL-17F),are secreted, structurally related proteins that share a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. IL-17 family proteins are proinflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Among IL-17 family members, IL-17D is most closely related to IL-17B, sharing 27% aa sequence homology. IL-17D is expressed preferentially in skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Like other IL-17 family members, IL-17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines including IL-6, IL-8, and GM-CSF. IL-17D has also been shown to suppress the proliferation of myeloid progenitors in colony formation assays.

Cysteine Protease ATG4A (ATG4A) is a cytoplasmic protein that belongs to the peptidase C54 family. ATG4A is widely expressed in many tissues at a low level, but the highest expression is observed in skeletal muscle and brain. ATG4A is a cysteine protease required for autophagy; it cleaves the C-terminal part of MAP1LC3, GABARAPL2 or GABARAP. ATG4A is inhibited by N-ethylmaleimide. It is suggested that ATG4A has a significant role in suppressing various cancers.

SMAD Family Member 1 (SMAD1) is a member of the dwarfin/SMAD family. SMAD1 has the highest expression in the heart and skeletal muscle, containing one MAD homology 1 domain and one MAD homology 2 domain, As a transcriptional modulator SMAD 1 is activated by bone morphogenetic proteins type 1 receptor kinase. Defects in SMAD1 may cause primary pulmonary hypertension (PPH1), characterized by plexiform lesions of proliferating endothelial cells in pulmonary arterioles. The lesions lead to elevated pulmonary arterial pression, right ventricular failure and death.

CMRF35-Like Molecule 9 (CD300LG) is a single-pass type I membrane protein which belongs to the CD300 family. CD300LG has one Ig-like V-type domain which mediates binding to lymphocyte. CD300LG is highly expressed in heart, skeletal muscle and placenta. CD300LG acts as a receptor which may mediate L-selectin-dependent lymphocyte rollings. CD300LG also binds SELL in a calcium dependent manner and lymphocyte. CD300LG may play a important role in molecular traffic across the capillary endothelium.

Microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B) is a member of the highly conserved ATG8 protein family. ATG8 proteins are present in all known eukaryotic organisms. MAP1LC3B is one of the four genes in the MAP1LC3 subfamily (others include MAP1LC3A, MAP1LC3C, and MAP1LC3B2). It is moat abundantly expressed in heart, brain, skeletal muscle and testis. LMAP1LC3B is a subunit of neuronal microtubule and functions in formation of autophagosomal vacuoles (autophagosomes). It associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. MAP1LC3B also plays a role in autophagy, a process that involves the bulk degradation of cytoplasmic component.

Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici

Her3, also called ErbB3, is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors.Her3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric Her3 serves as a low affinity receptor for the heregulins (HRG). HER3/ERBB3 Protein, Human, Recombinant (His & Avi), FITC-Labeled is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 71.6 kDa and the accession number is P21860-1.

Her3, also called ErbB3, is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors.Her3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric Her3 serves as a low affinity receptor for the heregulins (HRG). HER3/ERBB3 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 71.6 kDa and the accession number is P21860-1.

Neural Cell Adhesion Molecule 1 (NCAM-1), a multifunctional member of the immunoglobulin superfamily, is expressed on the surface of neurons, glia, skeletal muscle, and natural killer cells. NCAM-1 has been implicated as having a role in cell-cell adhesion, involved in development of the nervous system, and for cells involved in the expansion of T cells and dendritic cells which play an important role in immune surveillance. NCAM1 Protein, Human, Recombinant (aa 20-718, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 78.48 kDa and the accession number is P13591-2.