Description: Neuropeptides are regulators of synaptic transmission and their effects are mediated by G-protein coupled receptors. NPS (Neuropeptide S) is a 20 amino acid peptide cleaved from a larger precursor that contains a hydrophobic signal peptide and proteolytic cleavage processing sites. The N-terminal residue of NPS is always a serine regardless of the species. NPS is predominantly found in the central nervous system and plays an important role regulating sleep/wake functions, locomotion, arousal/anxiety responses and food intake. NPS functions by binding and activating its receptor, NPSR, and increasing intracellular calcium levels thereby acting as an excitatory transmitter. In addition, NPS stimulates the hypothalamo-pituitary adrenal (HPA) axis via the release of corticotropin-releasing factor (CRF) and arginine vasopressin (AVP). NPS and its receptor NPSR may also play a role in asthma pathogenesis.

Catalog Number: BOSSBS-11422R-HRP

UOM: 1 * 100 µl

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Description: Neuropeptides are regulators of synaptic transmission and their effects are mediated by G-protein coupled receptors. NPS (Neuropeptide S) is a 20 amino acid peptide cleaved from a larger precursor that contains a hydrophobic signal peptide and proteolytic cleavage processing sites. The N-terminal residue of NPS is always a serine regardless of the species. NPS is predominantly found in the central nervous system and plays an important role regulating sleep/wake functions, locomotion, arousal/anxiety responses and food intake. NPS functions by binding and activating its receptor, NPSR, and increasing intracellular calcium levels thereby acting as an excitatory transmitter. In addition, NPS stimulates the hypothalamo-pituitary adrenal (HPA) axis via the release of corticotropin-releasing factor (CRF) and arginine vasopressin (AVP). NPS and its receptor NPSR may also play a role in asthma pathogenesis.

Catalog Number: BOSSBS-11422R-A350

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Neuropeptides are regulators of synaptic transmission and their effects are mediated by G-protein coupled receptors. NPS (Neuropeptide S) is a 20 amino acid peptide cleaved from a larger precursor that contains a hydrophobic signal peptide and proteolytic cleavage processing sites. The N-terminal residue of NPS is always a serine regardless of the species. NPS is predominantly found in the central nervous system and plays an important role regulating sleep/wake functions, locomotion, arousal/anxiety responses and food intake. NPS functions by binding and activating its receptor, NPSR, and increasing intracellular calcium levels thereby acting as an excitatory transmitter. In addition, NPS stimulates the hypothalamo-pituitary adrenal (HPA) axis via the release of corticotropin-releasing factor (CRF) and arginine vasopressin (AVP). NPS and its receptor NPSR may also play a role in asthma pathogenesis.

Catalog Number: BOSSBS-11428R-CY7

UOM: 1 * 100 µl

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Description: RORET, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is a 465 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Found in all eukaryotes, members of the RBCC family typically function within a larger protein complex and possess ubiquitin-protein isopeptide ligase activity.The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The function of this protein has not been identified.

Catalog Number: BOSSBS-9160R

UOM: 1 * 100 µl

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Description: Cerebellin (CER), which was originally isolated from rat cerebellum, is a hexadecapeptide derived from a larger precursor called Cerebellin 1, also designated precerebellin 1 or Cbln1. Four propeptides, Cerebellin 1, Cerebellin 2 (Cbln2), Cerebellin 3 (Cbln3) and Cerebellin 4 (Cbln4), comprise the precerebellin subfamily within the C1q protein family. Cerebellin family members act as transneuronal regulators of synapse development and synaptic plasticity in various brain regions. Cerebellin and its metabolite, des-Ser(1)Cer, are also expressed in several extra-cerebellar tissues, including adrenal gland. Cerebellin 1, 2 and 3 assemble into homomeric and heteromeric complexes, thereby influencing each other’s degradation and secretion. Cerebellin 3 is not able to form homomeric complexes, and can only be secreted upon forming a heteromeric complex with Cerebellin 1. Decreased concentrations of Cerebellin have been found in the brain of patients with olivopontocerebellar atrophy (OPCA) and Shy-Drager syndrome, suggesting a role for Cerebellin in the pathology of these diseases.

Catalog Number: BOSSBS-11816R-FITC

UOM: 1 * 100 µl

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Description: Cerebellin (CER), which was originally isolated from rat cerebellum, is a hexadecapeptide derived from a larger precursor called Cerebellin 1, also designated precerebellin 1 or Cbln1. Four propeptides, Cerebellin 1, Cerebellin 2 (Cbln2), Cerebellin 3 (Cbln3) and Cerebellin 4 (Cbln4), comprise the precerebellin subfamily within the C1q protein family. Cerebellin family members act as transneuronal regulators of synapse development and synaptic plasticity in various brain regions. Cerebellin and its metabolite, des-Ser(1)Cer, are also expressed in several extra-cerebellar tissues, including adrenal gland. Cerebellin 1, 2 and 3 assemble into homomeric and heteromeric complexes, thereby influencing each other’s degradation and secretion. Cerebellin 3 is not able to form homomeric complexes, and can only be secreted upon forming a heteromeric complex with Cerebellin 1. Decreased concentrations of Cerebellin have been found in the brain of patients with olivopontocerebellar atrophy (OPCA) and Shy-Drager syndrome, suggesting a role for Cerebellin in the pathology of these diseases.

Catalog Number: BOSSBS-11537R

UOM: 1 * 100 µl

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Description: Cerebellin (CER), which was originally isolated from rat cerebellum, is a hexadecapeptide derived from a larger precursor Cerebellin 1, also designated precerebellin 1 or Cbln1. Four propeptides, Cerebellin 1, Cerebellin 2 (Cbln2), Cerebellin 3 (Cbln3), and Cerebellin 4 (Cbln4), comprise the precerebellin subfamily within the C1q protein family. Cerebellin family members act as transneuronal regulators of synapse development and synaptic plasticity in various brain regions. CER and it metabolite des-Ser1-cerebellin are also expressed in several extra-cerebellar tissues, including adrenal gland. Cerebellin 1, 2 and 3 assemble into homomeric and heteromeric complexes, thereby influencing each other’s degradation and secretion. Cerebellin 3 is not able to form homomeric complexes, and can only be secreted upon forming a heteromeric complex with Cerebellin 1. Decreased concentrations of CER has been found in the brain of patients with olivopontocerebellar atrophy (OPCA) and Shy-Drager syndrome, suggesting a role for CER in the pathology of these diseases.

Catalog Number: BOSSBS-11815R-A555

UOM: 1 * 100 µl

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Description: In contrast to the rapid early-onset weight gain seen in ob/ob mice (1-3), mutations in the tub gene lead to obesity gradually and strongly resemble late-onset obesity as seen in the human population (4). In addition to excessive deposition of adipose tissue, mice with the tub phenotype also suffer retinal degeneration and neurosensory hearing loss (4-6). The tripartite character of tubby phenotype is strikingly similar to human obesity syndromes such as Alstr鰉 (5) and Bardet-Biedl (6). A candidate for the tub gene has been described (4). A G芓 transversion in this candidate gene eliminates a donor splice site in the 3' coding region resulting in a larger transcript containing an unspliced intron (4). A second prematurely truncated mRNA transcript with the unspliced intron was found to be expressed in the brains of tubby mice at a 2-3 fold higher rate as compared to B6 mice (4). It has been postulated that the phenotypic features of tubby mice can be attributed to cellular apoptosis triggered by the expression of a mutated tub gene (4).

Catalog Number: BOSSBS-11536R-CY5

UOM: 1 * 100 µl

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Description: In contrast to the rapid early-onset weight gain seen in ob/ob mice (1-3), mutations in the tub gene lead to obesity gradually and strongly resemble late-onset obesity as seen in the human population (4). In addition to excessive deposition of adipose tissue, mice with the tub phenotype also suffer retinal degeneration and neurosensory hearing loss (4-6). The tripartite character of tubby phenotype is strikingly similar to human obesity syndromes such as Alstr鰉 (5) and Bardet-Biedl (6). A candidate for the tub gene has been described (4). A G芓 transversion in this candidate gene eliminates a donor splice site in the 3' coding region resulting in a larger transcript containing an unspliced intron (4). A second prematurely truncated mRNA transcript with the unspliced intron was found to be expressed in the brains of tubby mice at a 2-3 fold higher rate as compared to B6 mice (4). It has been postulated that the phenotypic features of tubby mice can be attributed to cellular apoptosis triggered by the expression of a mutated tub gene (4).

Catalog Number: BOSSBS-11536R-HRP

UOM: 1 * 100 µl

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Description: The Ras p21 family of guanine nucleotide proteins has been widely studied in view of its apparent role in signal transduction pathways and high frequency of mutations in human malignancies. It is now clear, however, that the Ras proteins (H-, K- and N-Ras p21) are members of a much larger superfamily of related proteins. Six members of this family, Rap 1A, Rap 1B, Rap 2, R-Ras, Ral A and Ral B, exhibit approximately 50% amino acid homology to Ras. The six mammalian Rho proteins (Rho A, B, C, G, 7 and 8) are approximately 30% homologous to Ras and are expressed in a wide range of cell types. Both Ras p21 and Rho p21, as well as other members of the Ras superfamily, contain a carboxy-terminal CAAX sequence (C, cysteine; A, aliphatic amino acid; X, any amino acid) which in the case of Ras has been shown to be essential for correct localization and function.

Catalog Number: BOSSBS-11583R-A647

UOM: 1 * 100 µl

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Description: Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjren syndrome and SLE (6).

Catalog Number: BOSSBS-7116R-A750

UOM: 1 * 100 µl

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Description: Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).

Catalog Number: BOSSBS-7116R-A555

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Ro autoantigens are of clinical significance because directed against them are found in most patients with primary Sjqgren syndrome, subacute cutaneous lupus erythematosus (SLE), neonatal lupus erythematosus, ANA-negative lupus erythematosus, and systemic lupus erythematosus-like disease secondary to homozygous C2 or C4 complement deficiency (1). Ro/SSA is a ribonucleoprotein that binds to auto in 35 to 50% of patients with SLE and in up to 97% of patients with Sjqgren syndrome (2). The Ro/SSA particle consists of a single immunoreactive protein noncovalently bound with one of four small RNA molecules (2). Most anti-Ro/SSA-positive sera detect not only the main protein, but also a smaller Ro/SSA protein (2). The genes which encode the smaller and larger proteins map to human chromosomes 11p15.5 and 1q31, respectively (3?). La/SSB is an autoimmune RNA-binding protein that plays a role in the transcription of RNA polymerase III was originally defined by its reactivity with auto from patients with Sjé°ƒren syndrome and SLE (6).

Catalog Number: BOSSBS-7116R-A647

UOM: 1 * 100 µl

Supplier: Bioss

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Description: In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Catalog Number: BOSSBS-13032R-A555

UOM: 1 * 100 µl

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Description: In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Catalog Number: BOSSBS-13032R-CY5

UOM: 1 * 100 µl

Supplier: Bioss

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Description: In mammalian cells, transcription is regulated in part by high molecular weight coactivating complexes that mediate signals between transcriptional activators and RNA polymerase (1). These complexes include CRSP (for cofactor required for Sp1 activation), which is required, in conjunction with TAFIIs, for transcriptional activation by Sp1 (2). CRSP is ubiquitously expressed in various tissues and functions as a multimeric complex that consists of nine distinct subunits (3). Several members of the CRSP family share sequence similarity with multiple components of the yeast transcriptional mediator proteins, including CRSP150, which is related to yeast Rgr1, and CRSP70, which is similar to the elongation factor TFIIS (4). CRSP77 and CRSP150 are also related to proteins within the putative murine mediator complex, while CRSP130 and CRSP34 are largely unrelated to either murine or yeast proteins (2,5). CRSP subunits also associate with larger multimeric coactivaor complexes, including ARC/DRI, which binds directly to SREBP and nuclear hormone receptors to facilitate transcription, and with NAT, a polymerase II-interacting complex that represses activated transcription (6,7).

Catalog Number: BOSSBS-11437R-CY7

UOM: 1 * 100 µl

Supplier: Bioss

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