1017 Results for: "single-use assemblies&amp"

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: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

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.

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: ProSci Inc.

DDX42 is a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX42 is a ATP-dependent RNA helicase. DDX42 binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. It also mediates RNA duplex formation thereby displacing the single-strand RNA binding protein.This gene encodes a member of the Asp-Glu-Ala-Asp (DEAD) box protein family. Members of this protein family are putative RNA helicases, and are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. Two transcript variants encoding the same protein have been identified for this gene.

Supplier: ProSci Inc.

Junctional Adhesion Molecule A (JAM-A) is a single-pass type I membrane protein that belongs to the immunoglobulin superfamily. JAM-A contains 2 Ig-like V-type (immunoglobulin-like) domains and Interacts with the ninth PDZ domain. JAM-A is localized to the tight junctions of both epithelial and endothelial cells. JAM-A seems to be involved in epithelial tight junction formation. JAM-A appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM-A, thereby preventing tight junction assembly. JAM-A plays a role in regulating monocyte transmigration involved in regulating integrity of the epithelial barrier. In the case of orthoreovirus infection, JAM-A serves as receptor for the virus.

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

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: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Bioss

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesises mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.

Supplier: Bioss

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesises mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.

Supplier: Bioss

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesises mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.

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: ProSci Inc.

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is an antigen recognized by autoimmune antibodies from a patient with watermelon stomach disease. This protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription.

Supplier: ProSci Inc.

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX21 encodes a DEAD box protein, which is an antigen recognized by autoimmune antibodies from a patient with watermelon stomach disease. This protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.

Supplier: Biotium

Recognizes a 67 kDa glycoprotein, which is identified as CD33. It is a transmembrane protein of the sialic acid-binding immunoglobulin-like lectin (Siglec) family. It belongs to the immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecules able of recruiting protein tyrosine phosphatases SHP-1 and SHP-2 to signal assemblies; these ITIMs are also used for ubiquitin-mediated removal of the receptor from the cell surface. CD33 is expressed on cells of myelomonocytic lineage, binds sialic acid residues in N- and O-glycans on cell surfaces, and is a therapeutic target for acute myeloid leukemia. CD33 is expressed on myeloid progenitors, monocytes, granulocytes, dendritic cells and mast cells. It is absent on platelets, lymphocytes, erythrocytes and hematopoietic stem cells.