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Bioss
Numéro de catalogue:
(BOSSBS-7852R-CY7)
Fournisseur:
Bioss
Description:
ZWINT is a component of the MIS12 complex, which is required for kinetochore function and spindle checkpoint activity. ZWINT interacts with ZW10 and targets it to the kinetochore at prometaphase. ZWINT is detectable on the kinetochore till late anaphase. Inhibition of ZWINT expression results in chromosome missegregation, spindle checkpoint failure and, ultimately, cell death upon cytokinesis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3738R-A680)
Fournisseur:
Bioss
Description:
Crkl is a 34kDa adaptor protein which has been shown to activate the RAS and JUN kinase signalling pathways and transforms fibroblasts in a RAS dependant manner. Crkl is a substitute of BCR ABL tyrosine kinase. In addition, Crkl has oncogenic potential.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7851R-CY7)
Fournisseur:
Bioss
Description:
Microtubules, polymers of alpha and beta tubulin subunits,form the mitotic spindle of a dividing cell and help to organizemembranous organelles during interphase. Katanin is a heterodimerthat consists of a 60 kDa ATPase (p60 subunit A 1) and an 80 kDaaccessory protein (p80 subunit B 1). The p60 subunit acts to severand disassemble microtubules, while the p80 subunit targets theenzyme to the centrosome. Katanin is a member of the AAA family ofATPases.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9164R-CY5)
Fournisseur:
Bioss
Description:
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11990R-A488)
Fournisseur:
Bioss
Description:
The HUNK (hormonally upregulated Neu-associated kinase) protein, also designated MAK-V in mouse, has been identified as a novel SNF1-related serine/threonine kinase. The human HUNK gene localizes to chromosome 21q22 and encodes a protein with nucleocytoplasmic distribution and localizes to the centrosome. Overexpression of the HUNK protein associates with approximately 50% of breast carcinomas, and may provide diagnostic-prognostic value as a molecular marker. Serine/threonine-protein kinase SNF1-like kinase 2 (SIK) phosphorylates Ser-794 of IRS1 in insulin-stimulated adipocytes, which may modulate the efficiency of insulin signal transduction. SIK is activated by phosphorylation on Thr-175 by STK11 in complex with STE20-related adapter-α and CAB39.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9166R-A488)
Fournisseur:
Bioss
Description:
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 protein localizes to cytoplasmic bodies. Its function has not been identified. Alternative splicing of this gene generates three transcript variants, named alpha, beta and gamma.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11990R-A350)
Fournisseur:
Bioss
Description:
The HUNK (hormonally upregulated Neu-associated kinase) protein, also designated MAK-V in mouse, has been identified as a novel SNF1-related serine/threonine kinase. The human HUNK gene localizes to chromosome 21q22 and encodes a protein with nucleocytoplasmic distribution and localizes to the centrosome. Overexpression of the HUNK protein associates with approximately 50% of breast carcinomas, and may provide diagnostic-prognostic value as a molecular marker. Serine/threonine-protein kinase SNF1-like kinase 2 (SIK) phosphorylates Ser-794 of IRS1 in insulin-stimulated adipocytes, which may modulate the efficiency of insulin signal transduction. SIK is activated by phosphorylation on Thr-175 by STK11 in complex with STE20-related adapter-α and CAB39.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5348R-CY7)
Fournisseur:
Bioss
Description:
PLM (FXYD1)is a member of a family of small membrane proteins that share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD and containing 7 invariant and 6 highly conserved amino acids. FXYD2, also known as the gamma subunit of the Na,K-ATPase, regulates the properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma), FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to induce channel activity in experimental expression systems. PLM may be phosphorylated by several kinases, including protein kinase A, protein kinase C, NIMA kinase, and myotonic dystrophy kinase. It is thought to form an ion channel or regulate ion channel activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9164R-FITC)
Fournisseur:
Bioss
Description:
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5347R-FITC)
Fournisseur:
Bioss
Description:
The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5348R-A488)
Fournisseur:
Bioss
Description:
PLM (FXYD1)is a member of a family of small membrane proteins that share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD and containing 7 invariant and 6 highly conserved amino acids. FXYD2, also known as the gamma subunit of the Na,K-ATPase, regulates the properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma), FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to induce channel activity in experimental expression systems. PLM may be phosphorylated by several kinases, including protein kinase A, protein kinase C, NIMA kinase, and myotonic dystrophy kinase. It is thought to form an ion channel or regulate ion channel activity.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9166R-CY3)
Fournisseur:
Bioss
Description:
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 protein localizes to cytoplasmic bodies. Its function has not been identified. Alternative splicing of this gene generates three transcript variants, named alpha, beta and gamma.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11988R-FITC)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11988R-HRP)
Fournisseur:
Bioss
Description:
Brain-specific neurabin I (neural tissue-specific F-actin binding protein I) is highly concentrated in the synapse of developed neurons; it localizes in the growth cone lamellipodia during neuronal development (1). Suppression of endogenous neurabin in rat hippocampal neurons inhibits neurite formation (1). Neurabin I recruits active PP1 via a PP1-docking sequence; mutation of the PP1-binding motif halts filopodia and restores stress fibers in neurabin I-expressing cells (2,3). Neurabin II (Spinophilin) is ubiquitously expressed but is abundantly expressed in brain (4). Neurabin II localizes to neuronal dentritic spines, which are the specialized protrusions from dendritic shafts that receive most of the excitatory input in the CNS (5). Neurabin II may regulate dendritic spine properties as neurabin II(-) mice have increased spine density during development in vitro and exhibit altered filopodial formation in cultured cells (5). Neurabin may also play a role in glutamatergic transmission as Neurabin II(-) mice exhibit reduced long-term depression and resistance to kainate-induced seizures and neronal apoptosis (5). Neurabin II complexes with the catalytic subunit of protein phosphatase-1 (PP1) in vitro thus modulating the activity of PP1 (4).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9164R-A488)
Fournisseur:
Bioss
Description:
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6944R-CY7)
Fournisseur:
Bioss
Description:
DEAD-box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure and ribosome/spliceosome assembly. Based on their distribution patterns, some members of this family may be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX32 is a 743 amino acid nuclear protein that localizes to the mitochondria and is a member of the DEAD box helicase family. Expressed in various tissues, DDX32 is up-regulated by ionomycin in T lymphocytes and down-regulated in acute lymphoblastic leukemia. Considered a novel RNA helicase, DDX32 may play an important role in the development of colorectal cancer and may be involved in regulating T-cell response to certain apoptotic stimuli.
UOM:
1 * 100 µl
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