1596 Risultati per: "single-use assemblies"

Supplier: Bioss

The MAGUK (membrane-associated guanylate kinase homologs) family of proteins contain multiple protein-binding domains and are involved in cell junction organization, tumor suppression, and signaling. The MAGUK family is divided into four subfamilies: DLG-like, ZO1-like, p55-like and LIN2-like. MPP7 (MAGUK p55 subfamily member 7), also known as palmitoylated membrane protein 7, is a 576 amino acid protein that belongs to the MAGUK family and assists in the assembly of protein complexes. A peripheral membrane protein that exists as a heterodimer, MPP7 enhances tight junction formation and epithelial cell polarity. MPP7 contains one SH3 domain, a guanylate kinase-like domain, two L27 domains and a single PDZ (DHR) domain. The gene encoding MPP7 maps to human chromosome 10p11.23

Supplier: Bioss

CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilisation and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinisation-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilisation.

Supplier: Bioss

CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.

Supplier: Bioss

CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.

Supplier: Bioss

Voltage-gated sodium channels are selective ion channels that regulate the permeability of sodium ions in excitable cells. During the propagation of an action potential, sodium channels allow an influx of sodium ions, which rapidly depolarizes the cell. Na+ CP type II beta(sodium channel, voltage-gated, type II, beta), also known as SCN2B, is a 215 amino acid single-pass type I membrane protein that plays a critical role in the expression and assembly of the heterotrimeric complex of the sodium channel and interacts with Tenascin-R to influence the clustering and regulation of sodium channels at nodes of Ranvier. Expressed specifically in brain, Na+ CP type II beta contains one Ig-like C2-type (immunoglobulin-like) domain and is encoded by a gene that maps to human chromosome 11q23.3 and mouse chromosome 9 A5.2.

Supplier: Bioss

Voltage-gated sodium channels are selective ion channels that regulate the permeability of sodium ions in excitable cells. During the propagation of an action potential, sodium channels allow an influx of sodium ions, which rapidly depolarizes the cell. Na+ CP type II beta(sodium channel, voltage-gated, type II, beta), also known as SCN2B, is a 215 amino acid single-pass type I membrane protein that plays a critical role in the expression and assembly of the heterotrimeric complex of the sodium channel and interacts with Tenascin-R to influence the clustering and regulation of sodium channels at nodes of Ranvier. Expressed specifically in brain, Na+ CP type II beta contains one Ig-like C2-type (immunoglobulin-like) domain and is encoded by a gene that maps to human chromosome 11q23.3 and mouse chromosome 9 A5.2.

Supplier: Bioss

The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells and is comprised of more than 100 different subunits. Many of the subunits belong to a family called nucleoporins (Nups), which are characterized by the presence of O-linked-N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). gp210, also known as Nup210 (nucleoporin 210kDa) or POM210, is a 1,887 amino acid single-pass type I membrane protein that localizes to both the endoplasmic reticulum and to the nucleus, specifically within the NPC. Expressed ubiquitously with highest expression in pancreas, testis, lung, ovary and liver, gp210 functions as a nucleoporin that is capable of dimerization and is essential for the assembly, fusion and structural integrity of the NPC. gp210 exists as multiple alternatively spliced isoforms and is subject to post-translational phosphorylation.

Supplier: Bioss

The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells and is comprised of more than 100 different subunits. Many of the subunits belong to a family called nucleoporins (Nups), which are characterized by the presence of O-linked-N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). gp210, also known as Nup210 (nucleoporin 210kDa) or POM210, is a 1,887 amino acid single-pass type I membrane protein that localizes to both the endoplasmic reticulum and to the nucleus, specifically within the NPC. Expressed ubiquitously with highest expression in pancreas, testis, lung, ovary and liver, gp210 functions as a nucleoporin that is capable of dimerization and is essential for the assembly, fusion and structural integrity of the NPC. gp210 exists as multiple alternatively spliced isoforms and is subject to post-translational phosphorylation.

Supplier: Bioss

EphB1, previously known as Elk (eph like kinase), is a receptor tyrosine kinase of the highly tissue restricted family of eph proteins. EphB1 and other ephB family members are type 1 membrane spanning proteins, comprised of immunoglobulin, fibronectin type III, and cysteine rich subdomains in the ecto domain, and the single uninterrupted cytoplasmic tyrosine kinase domain upstream of a carboxyterminal sterile alpha motif (SAM) domain. EphB family proteins bind ephrins of the B class. EphB1 is expressed predominately in developing neural structures in embryos, and in vascular epithelium of kidney, and other tissues. Upon binding to alternatively oligomerized ephrin B1, EphB1 signals regulation of cell attachment and cell to cell assembly. Members of this protein family are implicated in neuronal and vascular cell targeting.

Supplier: Bioss

CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.

Supplier: Bioss

CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.

Supplier: Bioss

Voltage-gated sodium channels are selective ion channels that regulate the permeability of sodium ions in excitable cells. During the propagation of an action potential, sodium channels allow an influx of sodium ions, which rapidly depolarizes the cell. Na+ CP type II beta(sodium channel, voltage-gated, type II, beta), also known as SCN2B, is a 215 amino acid single-pass type I membrane protein that plays a critical role in the expression and assembly of the heterotrimeric complex of the sodium channel and interacts with Tenascin-R to influence the clustering and regulation of sodium channels at nodes of Ranvier. Expressed specifically in brain, Na+ CP type II beta contains one Ig-like C2-type (immunoglobulin-like) domain and is encoded by a gene that maps to human chromosome 11q23.3 and mouse chromosome 9 A5.2.

Supplier: Bioss

The assembly of very-low-density lipoproteins (VLDLs) in the secretory apparatus of the hepatocyte relies on the mobilization of triacylglycerol (TAG) from the cytosolic pool by lipolysis and re-esterification. However, some of the re-esterified TAG products are returned to the cytosolic pool in the liver, which protects vulnerable body tissues from excess lipotoxic non-esterified fatty acids in the plasma. Some of the lipases involved in this process include arylacetamide deacetylase (AADAC) and its related proteins AADACL1 and AADACL2. AADAC, a single pass type II membrane protein of the endoplasmic reticulum, is expressed in hepatocytes, intestinal mucosal cells, pancreas and adrenal gland. It plays an important role in the metabolic activation of arylamine substrates to ultimate carcinogens. AADACL1 hydrolyzes the metabolic intermediate 2-acetyl monoalkylglycerol, and its inactivation results in disruption of ether lipid metabolism in cancer cells and impaired cell migration and tumor growth.

Supplier: Bioss

Component of the Integrator complex. The Integrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes. Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. The SOSS complex is required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent Signalling pathways. In the SOSS complex, it is required for the assembly of the complex and for stabilisation of the complex at DNA damage sites.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: GILSON LCMS

FC-204 Prep valve assembly package, for use with fraction collectors, Per: Fraction collectors

Supplier: Bioss

C4BPB is a member of a superfamily of proteins composed predominantly of tandemly arrayed short consensus repeats of approximately 60 amino acids. A single, unique beta-chain encoded by this gene assembles with seven identical alpha-chains into the predominant isoform of C4b-binding protein, a multimeric protein that controls activation of the complement cascade through the classical pathway. C4b-binding protein has a regulatory role in the coagulation system also, mediated through the beta-chain binding of protein S, a vitamin K-dependent protein that serves as a cofactor of activated protein C. The genes encoding both alpha and beta chains are located adjacent to each other on human chromosome 1 in the regulator of complement activation gene cluster. Alternative splicing gives rise to multiple transcript variants

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Peroxisomes are single-membrane bound organelles present in virtually all eukaryotic cells. They are involved in numerous catabolic and anabolic pathways, including beta-oxidation of very long chain fatty acids, metabolism of hydrogen peroxide, plasmalogen biosynthesis and bile acid synthesis. The Peroxin gene family, which includes more than 20 members, is required for peroxisome biogenesis. Peroxin 5R, also known as PEX5-related protein or Peroxisome biogenesis factor 5-like, is a 626 amino acid protein that is mainly expressed in brain, with some expression in testis and pancreas. Peroxin 5R contains five TPR repeats, which enable protein-protein interactions and assembly of large multiprotein complexes. There are three isoforms of Peroxin 5R that are produced as a result of alternative splicing events. These isoforms bind C-terminal peroxisome-targeting signals in a similar manner to Peroxin-5. Peroxin 5R interacts with Rab 8b, possibly playing a role in vesicular trafficking and neurotransmitter release.

Supplier: Bioss

CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Peroxisomes are single-membrane bound organelles present in virtually all eukaryotic cells. They are involved in numerous catabolic and anabolic pathways, including beta-oxidation of very long chain fatty acids, metabolism of hydrogen peroxide, plasmalogen biosynthesis and bile acid synthesis. The Peroxin gene family, which includes more than 20 members, is required for peroxisome biogenesis. Peroxin 5R, also known as PEX5-related protein or Peroxisome biogenesis factor 5-like, is a 626 amino acid protein that is mainly expressed in brain, with some expression in testis and pancreas. Peroxin 5R contains five TPR repeats, which enable protein-protein interactions and assembly of large multiprotein complexes. There are three isoforms of Peroxin 5R that are produced as a result of alternative splicing events. These isoforms bind C-terminal peroxisome-targeting signals in a similar manner to Peroxin-5. Peroxin 5R interacts with Rab 8b, possibly playing a role in vesicular trafficking and neurotransmitter release.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.

Supplier: Bioss

Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments. V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends. These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively. This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC. The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint. May also be required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ.