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Catalog Number: (BOSSBS-3349R-CY5)
Supplier: Bioss
Description: postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-A350)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-A488)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-A750)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localise to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localisation. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-HRP)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-CY3)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-A647)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3349R-A680)
Supplier: Bioss
Description: postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3349R-CY5.5)
Supplier: Bioss
Description: postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM: 1 * 100 µl


Catalog Number: (PRSI29-573)
Supplier: ProSci Inc.
Description: AK3L1 is a member of the adenylate kinase family of enzymes. The protein is localized to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide compositions within a cell by catalyzing the reversible transfer of phosphate group among these nucleotides.This gene encodes a member of the adenylate kinase family of enzymes. The encoded protein is localized to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide compositions within a cell by catalyzing the reversible transfer of phosphate group among these nucleotides. Five isozymes of adenylate kinase have been identified in vertebrates. Expression of these isozymes is tissue-specific and developmentally regulated. A pseudogene for this gene has been located on chromosome 17. Three transcript variants encoding the same protein have been identified for this gene. Sequence alignment suggests that the gene defined by NM_013410, NM_203464, and NM_001005353 is located on chromosome 1.
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-3349R-HRP)
Supplier: Bioss
Description: postsynaptic density protein 95 is a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway. This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with DLG2. With DLG2 it is recruited into the same NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6175R-A555)
Supplier: Bioss
Description: Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by Guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
UOM: 1 * 100 µl


Catalog Number: (PRSI26-565)
Supplier: ProSci Inc.
Description: DCP1B may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It may remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.DCP1B is a core component of the mRNA decapping complex, a key factor in the regulation of mRNA decay (Lykke-Andersen, 2002 [PubMed 12417715]).
UOM: 1 * 50 µG


Catalog Number: (BOSSBS-3712R-CY7)
Supplier: Bioss
Description: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13283R-CY3)
Supplier: Bioss
Description: GAPVD1 is a 1478 amino acid peripheral membrane protein that acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF). GAPVD1 participates in many processes such as insulin receptor internalization, Glut4 trafficking and endocytosis. In addition, depletion of GAPVD1 leads to delayed EGFR degradation by mediating receptor ubiquination through its RGD domain, suggesting that it may be an important mediator of carcinogenesis resulting from Ras protein mutations. There are six isoforms of GAPVD1 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13283R-FITC)
Supplier: Bioss
Description: GAPVD1 is a 1478 amino acid peripheral membrane protein that acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF). GAPVD1 participates in many processes such as insulin receptor internalization, Glut4 trafficking and endocytosis. In addition, depletion of GAPVD1 leads to delayed EGFR degradation by mediating receptor ubiquination through its RGD domain, suggesting that it may be an important mediator of carcinogenesis resulting from Ras protein mutations. There are six isoforms of GAPVD1 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


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