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Catalog Number: (BOSSBS-13527R-A680)
Supplier: Bioss
Description: G protein-coupled receptors (GPRs) are a protein family of transmembrane receptors that transmit an extracellular signal (ligand binding) into an intracellular signal (G protein activation). GPR signaling is an ancient evolutionarily mechanism used by all eukaryotes to sense environmental stimuli and mediate cell-cell communication. GPRs have seven membrane-spanning domains and the extracellular domains are often glycosylated. These extracellular loops also contain two highly conserved cysteine residues which create disulfide bonds to stabilize the receptor structure. GPR26 (G-protein coupled receptor 26) is a 337 amino acid protein that is primarily expressed in regions of the brain. GPR26 is characterized as an orphan? G protein-coupled receptor, which is a receptor that binds an unidentified natural ligand. Due to evidence of GPR26 being downregulated in glioblastomas, it has been suggested that GPR26 may be a suppressor of early glioma development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11281R-HRP)
Supplier: Bioss
Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7121R)
Supplier: Bioss
Description: The RAD23 gene of Saccharomyces cerevisiae is required for excision-repair of UV damaged DNA (1). RAD23 resembles the other DNA repair genes, RAD2, RAD6, RAD7, RAD18, and RAD54, all of which also exhibit increased transcription in response to DNA damage and during meiosis (2). RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function (3). RAD23 bears a ubiquitin-like domain at its amino terminus and this ubiquitin-like domain affects protein function in a nonproteolytic manner (3). Rad23 is a highly conserved protein involved in nucleotide excision repair (NER) that associates with the proteasome via its amino-terminus (4). Its carboxy-terminal ubiquitin-associated domain is evolutionarily conserved from yeast to humans (4). In addition to a role in DNA repair events in yeast, several lines of evidence indicate that the Rad23 protein may regulate the activity of the 26 S proteasome (5).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13527R-A647)
Supplier: Bioss
Description: G protein-coupled receptors (GPRs) are a protein family of transmembrane receptors that transmit an extracellular signal (ligand binding) into an intracellular signal (G protein activation). GPR signaling is an ancient evolutionarily mechanism used by all eukaryotes to sense environmental stimuli and mediate cell-cell communication. GPRs have seven membrane-spanning domains and the extracellular domains are often glycosylated. These extracellular loops also contain two highly conserved cysteine residues which create disulfide bonds to stabilize the receptor structure. GPR26 (G-protein coupled receptor 26) is a 337 amino acid protein that is primarily expressed in regions of the brain. GPR26 is characterized as an ‘orphan’ G protein-coupled receptor, which is a receptor that binds an unidentified natural ligand. Due to evidence of GPR26 being downregulated in glioblastomas, it has been suggested that GPR26 may be a suppressor of early glioma development.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1766R-A647)
Supplier: Bioss
Description: Follicular dendritic cells are cells that facilitate antigen recognition by B cells in follicles. This kind of dendritic cell is not bone marrow derived and is not a kind of blood cell. It is purely a resident of the follicles of secondary lymphoid organs. B cells form germinal centers around follicular dendritic cells in lymphoid organs. Dendritic cells form from monocytes, white blood cells which circulate in the body and, depending on the right signal, can turn into dendritic cells or macrophages. The monocytes in turn are formed from stem cells in the bone marrow.In normal tissue this antibody identifies dendritic cells and a proportion of B lymphocytes. Evidence in pathological tissue and functional studies suggests it binds to an epitope expressed by antigen presenting cells. Within the macrophage/dendritic cell populations the epitope seen by RFD1 is coexpressed with RFD7 by a subset of cells that exhibit suppressive activity on T cell stimulation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7121R-CY5)
Supplier: Bioss
Description: The RAD23 gene of Saccharomyces cerevisiae is required for excision-repair of UV damaged DNA (1). RAD23 resembles the other DNA repair genes, RAD2, RAD6, RAD7, RAD18, and RAD54, all of which also exhibit increased transcription in response to DNA damage and during meiosis (2). RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function (3). RAD23 bears a ubiquitin-like domain at its amino terminus and this ubiquitin-like domain affects protein function in a nonproteolytic manner (3). Rad23 is a highly conserved protein involved in nucleotide excision repair (NER) that associates with the proteasome via its amino-terminus (4). Its carboxy-terminal ubiquitin-associated domain is evolutionarily conserved from yeast to humans (4). In addition to a role in DNA repair events in yeast, several lines of evidence indicate that the Rad23 protein may regulate the activity of the 26 S proteasome (5).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7121R-CY3)
Supplier: Bioss
Description: The RAD23 gene of Saccharomyces cerevisiae is required for excision-repair of UV damaged DNA (1). RAD23 resembles the other DNA repair genes, RAD2, RAD6, RAD7, RAD18, and RAD54, all of which also exhibit increased transcription in response to DNA damage and during meiosis (2). RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function (3). RAD23 bears a ubiquitin-like domain at its amino terminus and this ubiquitin-like domain affects protein function in a nonproteolytic manner (3). Rad23 is a highly conserved protein involved in nucleotide excision repair (NER) that associates with the proteasome via its amino-terminus (4). Its carboxy-terminal ubiquitin-associated domain is evolutionarily conserved from yeast to humans (4). In addition to a role in DNA repair events in yeast, several lines of evidence indicate that the Rad23 protein may regulate the activity of the 26 S proteasome (5).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12003R)
Supplier: Bioss
Description: Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors (1). Each of a very broad range of receptors specifically detects an extracellular stimulus (a photon, pheromone, odorant, hormone or neurotransmitter) while the effectors (e.g., adenyl cyclase), which act to generate one or more intracellular messengers, are less numerous. In mammals, G protein alpha, beta and gamma polypeptides are encoded by at least 16, 4 and 7 genes, respectively (2-5). Most interest in G proteins has been focused on their alpha subunits, since these proteins bind and hydrolyze GTP and most obviously regulate the activity of the best studied effectors. More recent evidence, however, has established an important regulatory role for the beta gamma subunits (6-8). The Gs subfamily of G alpha subunits includes two closely related proteins, Ga s and Ga olf, which respectively stimulate adenylate cyclase and mediate response to olfactory stimuli (9).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13647R-A555)
Supplier: Bioss
Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13647R-A488)
Supplier: Bioss
Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13647R-FITC)
Supplier: Bioss
Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4168R-A555)
Supplier: Bioss
Description: TNIK is a MSN protein kinase that interacts with both TNF receptor-associated factor 2 (TRAF2) and the adapter protein NCK. The protein has been shown to activate the c-Jun N-terminal kinase pathway when over expressed in Phoenix-A cells. TNIK has been shown to phosphorylate gelsolin, the principal intracellular and extracellular actin-severing protein, in vitro. This and evidence from mutational studies suggest that TNIK functions in the regulation of the cytoskeleton. Northern analysis indicates TNIK expression in human heart, skeletal muscle, and brain, with lower levels of expression in kidney, liver, lung, and pancreas. ESTs have been isolated from human tissue libraries, including normal amnion, gallbladder and skin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-4168R-FITC)
Supplier: Bioss
Description: TNIK is a MSN protein kinase that interacts with both TNF receptor-associated factor 2 (TRAF2) and the adapter protein NCK. The protein has been shown to activate the c-Jun N-terminal kinase pathway when over expressed in Phoenix-A cells. TNIK has been shown to phosphorylate gelsolin, the principal intracellular and extracellular actin-severing protein, in vitro. This and evidence from mutational studies suggest that TNIK functions in the regulation of the cytoskeleton. Northern analysis indicates TNIK expression in human heart, skeletal muscle, and brain, with lower levels of expression in kidney, liver, lung, and pancreas. ESTs have been isolated from human tissue libraries, including normal amnion, gallbladder and skin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12412R-CY7)
Supplier: Bioss
Description: Sp1 is a sequence-specific transcription factor that recognizes GGGGCGGGGC and closely related sequences, which are often referred to as GC boxes. Sp1 was initially identified as a HeLa cell-derived factor that selectively activates in vitro transcription from the SV40 promoter and binds to the multiple GC boxes in the 21-bp repeated elements in SV40. The sequence specificity of DNA binding is conferred by Zn (II) fingers, whereas a different region of Sp1 appears to regulate the affinity of DNA binding. Sp1 belongs to a subgroup of transcription factors that are phosphorylated upon binding to promoter sequences. Evidence suggests that the early growth response gene, Erg-1 (also known as Zif268 or NGF1-A) (7), may downregulate certain mammalian gene promoters by competing with Sp1 for binding to an overlapping binding motif. The gene encoding human Sp1 maps to chromosome 12q13.1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12412R-A555)
Supplier: Bioss
Description: Sp1 is a sequence-specific transcription factor that recognizes GGGGCGGGGC and closely related sequences, which are often referred to as GC boxes. Sp1 was initially identified as a HeLa cell-derived factor that selectively activates in vitro transcription from the SV40 promoter and binds to the multiple GC boxes in the 21-bp repeated elements in SV40. The sequence specificity of DNA binding is conferred by Zn (II) fingers, whereas a different region of Sp1 appears to regulate the affinity of DNA binding. Sp1 belongs to a subgroup of transcription factors that are phosphorylated upon binding to promoter sequences. Evidence suggests that the early growth response gene, Erg-1 (also known as Zif268 or NGF1-A) (7), may downregulate certain mammalian gene promoters by competing with Sp1 for binding to an overlapping binding motif. The gene encoding human Sp1 maps to chromosome 12q13.1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11281R-CY3)
Supplier: Bioss
Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).
UOM: 1 * 100 µl


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