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Anticorps
Numéro de catalogue:
(BOSSBS-6796R-A680)
Fournisseur:
Bioss
Description:
Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9491R-CY5.5)
Fournisseur:
Bioss
Description:
The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12066R-A750)
Fournisseur:
Bioss
Description:
Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels that mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs, including barbiturates, anaesthetics and benzodiazepines.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5104R-A488)
Fournisseur:
Bioss
Description:
Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8682R-A750)
Fournisseur:
Bioss
Description:
The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilise the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilised antigen based chromatography.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8682R-FITC)
Fournisseur:
Bioss
Description:
The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8682R-A647)
Fournisseur:
Bioss
Description:
The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6992R-CY5)
Fournisseur:
Bioss
Description:
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3214R-CY5.5)
Fournisseur:
Bioss
Description:
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3214R-CY3)
Fournisseur:
Bioss
Description:
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11067R-FITC)
Fournisseur:
Bioss
Description:
Beta-tectorin is a 329 amino acid secreted protein that contains one zona pellucida (ZP) domain. While it may form homomeric filaments after self-association, Beta-tectorin may also form heteromeric filaments when it associates with ?tectorin. The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia and proteolytically released into the extracellular compartment. Beta-tectorin is one of the major non-collagenous components of the tectorial membrane. The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3944R-A350)
Fournisseur:
Bioss
Description:
GNG2 (Guanine nucleotide binding protein (G protein), gamma 2) is a member of the guanine nucleotide-binding proteins (G proteins) family. Heterotrimeric G proteins are involved as a modulator or transducer in various transmembrane signaling systems. The specificity of a G protein-receptor interaction is primarily mediated by the gamma subunit.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11483R-A488)
Fournisseur:
Bioss
Description:
Semaphorins are a family of cell surface and secreted proteins involved in neural development that are conserved from insects to humans. Members of this family are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular “semaphorin†domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterized by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. SEMA6C, also known as SEMA Y, is a transmembrane protein expressed in fetal brain and adult skeletal muscle. Three isoforms of this semaphorin exist due to alternative splicing: SEMA6C 1, SEMA6C 2 and SEMA6C 3. The extracellular domain of SEMA6C induces growth cone collapse of dorsal root ganglion and plays a role in generation or stability of entorhino-hippocampal synapses.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1540R-A488)
Fournisseur:
Bioss
Description:
Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2173R-CY7)
Fournisseur:
Bioss
Description:
The Olfactomedin family comprises a diverse group of secreted glycoproteins, which includes OLFM1 (Noelin-1), OLFM2 (Noelin-2), OLFM3 (Noelin-3), OLFM4 (Noelin-4), tiarin, pancortin, gliomedin and mycocilin. These proteins are implicated in the development of the nervous system. Specifically, OLFM1 and OLFM2 expression is observed in the neural plate and neural crest, as well as in the cranial ganglia in mouse at E8-10, and later in brain tissue and in the zone of polarizing activity in the limb. Overexpression of OLFM1 causes an excess of neural crest emigrations and prolonged neural crest production. OLFM2 participates in the regulation of the development of the anterior nervous system. An Arg144Gln mutation in OLFM2 has been implicated as a possible cause for open-angle glaucoma (OAG).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2173R-A750)
Fournisseur:
Bioss
Description:
The Olfactomedin family comprises a diverse group of secreted glycoproteins, which includes OLFM1 (Noelin-1), OLFM2 (Noelin-2), OLFM3 (Noelin-3), OLFM4 (Noelin-4), tiarin, pancortin, gliomedin and mycocilin. These proteins are implicated in the development of the nervous system. Specifically, OLFM1 and OLFM2 expression is observed in the neural plate and neural crest, as well as in the cranial ganglia in mouse at E8-10, and later in brain tissue and in the zone of polarising activity in the limb. Overexpression of OLFM1 causes an excess of neural crest emigrations and prolonged neural crest production. OLFM2 participates in the regulation of the development of the anterior nervous system. An Arg144Gln mutation in OLFM2 has been implicated as a possible cause for open-angle glaucoma (OAG).
UOM:
1 * 100 µl
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