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Catalog Number: (BOSSBS-0299R-CY5)
Supplier: Bioss
Description: Adenylate kinase is an enzyme involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate group among adinine nucleotides. Three isozymes of adenylate kinase have been identified in vertebrates, adenylate isozyme 1 (AK1), 2 (AK2) and 3 (AK3). AK1 is found in the cytosol of skeletal muscle, brain and erythrocytes, whereas AK2 and AK3 are found in the mitochondria of other tissues including liver and heart. AK1 was identified because of its association with a rare genetic disorder causing nonspherocytic hemolytic anemia where a mutation in the AK1 gene was found to reduce the catalytic activity of the enzyme. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11337R-A488)
Supplier: Bioss
Description: C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages are the primary source of C1q, while anti-inflammatory drugs as well as cytokines differentially regulate expression of the mRNA, as well as the protein. However, its ability to modulate the interaction of platelets with collagen and immune complexes suggests C1q influences homeostasis as well as other immune activities, and perhaps thrombotic complications resulting from immune injury. Defects in C1q-A, C1q-B and C1q-C cause inactivation of the classical pathway, leading to a rare genetic disorder characterized by lupus-like symptoms.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11337R-CY5)
Supplier: Bioss
Description: C1q, a subcomponent of the classical complement pathway, is composed of nine subunits that mediate classical complement activation and thereby play an important role in the immune response. Six of these subunits are disulfide-linked dimers of chains A and B, while three of these subunits, designated C1q-A through C1q-C, are disulfide-linked dimers of chain C. The presence of receptors for C1q on effector cells modulates its activity, which may be antibody-dependent or independent. Macrophages are the primary source of C1q, while anti-inflammatory drugs as well as cytokines differentially regulate expression of the mRNA, as well as the protein. However, its ability to modulate the interaction of platelets with collagen and immune complexes suggests C1q influences homeostasis as well as other immune activities, and perhaps thrombotic complications resulting from immune injury. Defects in C1q-A, C1q-B and C1q-C cause inactivation of the classical pathway, leading to a rare genetic disorder characterized by lupus-like symptoms.
UOM: 1 * 100 µl


Supplier: Biotium
Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Supplier: Biotium
Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Supplier: Biotium
Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Catalog Number: (BOSSBS-11455R-A750)
Supplier: Bioss
Description: Lissencephaly (smooth brain) is an abnormality of brain development characterised by incomplete neuronal migration and a smooth cerebral surface, manifesting as severe mental retardation. Genetic analysis has identified two proteins that are mutated in some cases of lissencephaly, designated lissencephaly-1 protein (LIS1) and doublecortin. LIS1 displays sequence homology to subunits of heterotrimeric G proteins, and doublecortin contains a consensus Abl phosphorylation site. In addition, the DCAMKL1 (doublecortin-like and CAM kinase-like 1) protein shows homology to doublecortin. All three proteins are highly expressed in developing brain and may function together to regulate microtubules involved in neuronal migration. The DCAMKL1 protein encodes a functional kinase that is capable of phosphorylating myelin basic protein and itself, but its kinase activity does not appear to affect its microtubule polymerization activity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11512R-CY7)
Supplier: Bioss
Description: Bardet-Biedl syndrome (BBS) is a pleiotropic genetic disorder characterized by obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnormalities, and developmental delay. Other associated clinical findings in BBS patients include diabetes, hypertension, and congenital heart defects. BBS genes map to multiple loci and encode fourteen proteins, BBS1-BBS14. Many BBS genes encode basal body or cilia proteins, suggesting that BBS is a ciliary dysfunction disorder. BBS10 (Bardet-Biedl syndrome 10), also known as chromosome 12 open reading fame 58, C12orf58 or FLJ23560, is a novel 723 amino acid protein belonging to the TCP-1 chaperonin family. BBS10 localizes to the basal body of primary cilium and assists in protein folding upon ATP hydrolysis. Inhibition of BBS10 has been found to impair ciliogenesis, activate the glycogen synthase kinase 3 pathway and cause peroxisome proliferator-activated receptor nuclear accumulation. The gene encoding BBS10 contains two exons and maps to human chromosome 12q21.2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11512R-A647)
Supplier: Bioss
Description: Bardet-Biedl syndrome (BBS) is a pleiotropic genetic disorder characterized by obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnormalities, and developmental delay. Other associated clinical findings in BBS patients include diabetes, hypertension, and congenital heart defects. BBS genes map to multiple loci and encode fourteen proteins, BBS1-BBS14. Many BBS genes encode basal body or cilia proteins, suggesting that BBS is a ciliary dysfunction disorder. BBS10 (Bardet-Biedl syndrome 10), also known as chromosome 12 open reading fame 58, C12orf58 or FLJ23560, is a novel 723 amino acid protein belonging to the TCP-1 chaperonin family. BBS10 localizes to the basal body of primary cilium and assists in protein folding upon ATP hydrolysis. Inhibition of BBS10 has been found to impair ciliogenesis, activate the glycogen synthase kinase 3 pathway and cause peroxisome proliferator-activated receptor nuclear accumulation. The gene encoding BBS10 contains two exons and maps to human chromosome 12q21.2.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0299R-A647)
Supplier: Bioss
Description: Adenylate kinase is an enzyme involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate group among adinine nucleotides. Three isozymes of adenylate kinase have been identified in vertebrates, adenylate isozyme 1 (AK1), 2 (AK2) and 3 (AK3). AK1 is found in the cytosol of skeletal muscle, brain and erythrocytes, whereas AK2 and AK3 are found in the mitochondria of other tissues including liver and heart. AK1 was identified because of its association with a rare genetic disorder causing nonspherocytic hemolytic anemia where a mutation in the AK1 gene was found to reduce the catalytic activity of the enzyme. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5707R-CY7)
Supplier: Bioss
Description: TUSC2/FUS1 is a novel tumor suppressor gene identified in the human chromosome 3p21.3 region where allele losses and genetic alterations occur early and frequently for many human cancers. Expression of TUSC2 protein is absent or reduced in the majority of lung cancers and premalignant lung lesions. Restoration of TUSC2 function in 3p21.3-deficient non-small cell lung carcinoma cells significantly inhibits tumor cell growth by induction of apoptosis and alteration of cell cycle kinetics. TUSC2 may induce apoptosis through the activation of the intrinsic mitochondrial-dependent and Apaf-1-associated pathways and inhibit the function of protein tyrosine kinases including EGFR, PDGFR, AKT, c-Abl, and c-Kit.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3305R-CY5)
Supplier: Bioss
Description: N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate-gated ion channels. These receptors have been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C) and NMDAR2D (GRIN2D). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3305R-FITC)
Supplier: Bioss
Description: N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate-gated ion channels. These receptors have been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C) and NMDAR2D (GRIN2D). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8566R-CY7)
Supplier: Bioss
Description: N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8566R-A555)
Supplier: Bioss
Description: N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5382R-A555)
Supplier: Bioss
Description: N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of three different subunits: NR1 (GRIN1), NR2 (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The NR2 subunit acts as the agonist binding site for glutamate. This receptor is the predominant excitatory neurotransmitter receptor in the mammalian brain. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222
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