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Numéro de catalogue: (BOSSBS-13642R-A488)

Fournisseur:  Bioss
Description:   Many growth factors function by binding receptors with intrinsic tyrosine kinase activity (1,2). Signaling by such receptors involves a series of intermediates characterized by SH2 domains that bind tyrosine phosphorylated receptors by a direct interaction between the SH2 domain and the phosphotyrosine-containing receptor sequences (3,4). GRB7, a SH2 domain protein, has a single SH2 domain at its C-terminal, a central region with similarity to Ras GAP and a proline-rich N-terminus (5,6). GRB7 maps to the region on mouse chromosome 11 containing the Neu gene (6). This region of mouse chromosome 11 is syntenic to an area of human chromosome 17q that is frequently amplified in breast cancer (6,7). Moreover, GRB7 is amplified and over-expressed in breast cancer and is found in a complex with Neu gp185 (6).
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13642R-A350)

Fournisseur:  Bioss
Description:   Many growth factors function by binding receptors with intrinsic tyrosine kinase activity (1,2). Signaling by such receptors involves a series of intermediates characterized by SH2 domains that bind tyrosine phosphorylated receptors by a direct interaction between the SH2 domain and the phosphotyrosine-containing receptor sequences (3,4). GRB7, a SH2 domain protein, has a single SH2 domain at its C-terminal, a central region with similarity to Ras GAP and a proline-rich N-terminus (5,6). GRB7 maps to the region on mouse chromosome 11 containing the Neu gene (6). This region of mouse chromosome 11 is syntenic to an area of human chromosome 17q that is frequently amplified in breast cancer (6,7). Moreover, GRB7 is amplified and over-expressed in breast cancer and is found in a complex with Neu gp185 (6).
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11619R-A750)

Fournisseur:  Bioss
Description:   Members of the RTP (receptor transporter proteins) family have recently been discovered to influence bitter taste receptor expression in addition to inducing the expression of mammalian odorant receptors. RTP3 is a 232 amino acid single-pass type III membrane protein belonging to the TMEM7 family. Unlike other RTP proteins, RTP3 is not expressed in olfactory neurons but is expressed predominantly in liver. RTP3 is involved in the functional expression of bitter taste receptors and suppresses cell proliferation, and is also found in human circumvallate papillae and testis (regions where bitter taste receptors are expressed). The gene encoding RTP3 maps to human chromosome 3p21.31 within C3CER1 (chromosome 3 common eliminated region 1), which is frequently eliminated in chromosomal deletions of solid tumours.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11619R-CY3)

Fournisseur:  Bioss
Description:   Members of the RTP (receptor transporter proteins) family have recently been discovered to influence bitter taste receptor expression in addition to inducing the expression of mammalian odorant receptors. RTP3 is a 232 amino acid single-pass type III membrane protein belonging to the TMEM7 family. Unlike other RTP proteins, RTP3 is not expressed in olfactory neurons but is expressed predominantly in liver. RTP3 is involved in the functional expression of bitter taste receptors and suppresses cell proliferation, and is also found in human circumvallate papillae and testis (regions where bitter taste receptors are expressed). The gene encoding RTP3 maps to human chromosome 3p21.31 within C3CER1 (chromosome 3 common eliminated region 1), which is frequently eliminated in chromosomal deletions of solid tumors.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11619R-A488)

Fournisseur:  Bioss
Description:   Members of the RTP (receptor transporter proteins) family have recently been discovered to influence bitter taste receptor expression in addition to inducing the expression of mammalian odorant receptors. RTP3 is a 232 amino acid single-pass type III membrane protein belonging to the TMEM7 family. Unlike other RTP proteins, RTP3 is not expressed in olfactory neurons but is expressed predominantly in liver. RTP3 is involved in the functional expression of bitter taste receptors and suppresses cell proliferation, and is also found in human circumvallate papillae and testis (regions where bitter taste receptors are expressed). The gene encoding RTP3 maps to human chromosome 3p21.31 within C3CER1 (chromosome 3 common eliminated region 1), which is frequently eliminated in chromosomal deletions of solid tumors.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Neuroglycan C is a brain-specific chondroitin sulfate proteoglycan (CSPG) implicated in the proliferation of neural stem and progenitor cells. Neuro-glycan C is a single-pass membrane protein that can manifest as a part-time proteoglycan depending on the tissue expressing it. In its proteoglycan form, Neuroglycan C exhibits chondroitin sulfate glycans and functions as a receptor for midkine, a growth factor that binds heparin, to affect cytoskeletal changes. By means of ectodomain shedding, the ectodomain of Neuroglycan C is able to enhance neurite outgrowth from neurons. Neurite growth stimulation is affected by both an EGF-like and an acidic amino acid domain found on the shed ectodomain. Both domains instigate neurite growth, however, these domains exhibit differing functionality as to number of neurites produced and neuron types stimulated.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11070R-A350)

Fournisseur:  Bioss
Description:   The amphoterin-induced gene and ORF (AMIGO) family of proteins consists of AMIGO-1, AMIGO-2 and AMIGO-3. All three members are single pass type I membrane proteins that contain several leucine-rich repeats, one IgG domain, and a transmembrane domain. The AMIGO proteins are specifically expressed on fiber tracts of neuronal tissues and participate in their formation. The AMIGO proteins can form complexes with each other, but can also bind itself. AMIGO-1, also designated Alivin-2, promotes growth and fasciculation of neurites and plays a role in myelination and fasciculation of developing neural axons. In cerebellar neurons, AMIGO-2 (Alivin-1) is crucial for depolarization-dependent survival. Similar to AMIGO-1 and AMIGO-2, AMIGO-3 (Alivin-3) plays a role in homophilic and/or heterophilic cell-cell interaction and signal transduction.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11070R-A488)

Fournisseur:  Bioss
Description:   The amphoterin-induced gene and ORF (AMIGO) family of proteins consists of AMIGO-1, AMIGO-2 and AMIGO-3. All three members are single pass type I membrane proteins that contain several leucine-rich repeats, one IgG domain, and a transmembrane domain. The AMIGO proteins are specifically expressed on fiber tracts of neuronal tissues and participate in their formation. The AMIGO proteins can form complexes with each other, but can also bind itself. AMIGO-1, also designated Alivin-2, promotes growth and fasciculation of neurites and plays a role in myelination and fasciculation of developing neural axons. In cerebellar neurons, AMIGO-2 (Alivin-1) is crucial for depolarization-dependent survival. Similar to AMIGO-1 and AMIGO-2, AMIGO-3 (Alivin-3) plays a role in homophilic and/or heterophilic cell-cell interaction and signal transduction.
UOM:  1 * 100 µl
Fournisseur:  Biotium
Description:   This antibody recognizes a glycoprotein of 75 kDa, identified as low affinity Nerve Growth Factor (NGF) Receptor (p75NGFR) or Neurotrophin Receptor (p75NTR). Its epitope spans in aa 1-160 of extracellular domain of NGFR/NTR. NGF-receptor contains an extracellular domain containing four 40-amino acid repeats with 6 cysteine residues at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155-amino acid cytoplasmic domain. The cysteine-rich region contains the nerve growth factor binding domain. NGF is important for the development, differentiation, and survival of variety of neuronal and non-neuronal cells. Its action is mediated by binding two distinct receptors, the high affinity p140 and low affinity p75.
Fournisseur:  Biotium
Description:   This antibody recognizes a glycoprotein of 75 kDa, identified as low affinity Nerve Growth Factor (NGF) Receptor (p75NGFR) or Neurotrophin Receptor (p75NTR). Its epitope spans in aa 1-160 of extracellular domain of NGFR/NTR. NGF-receptor contains an extracellular domain containing four 40-amino acid repeats with 6 cysteine residues at conserved positions followed by a serine/threonine-rich region, a single transmembrane domain, and a 155-amino acid cytoplasmic domain. The cysteine-rich region contains the nerve growth factor binding domain. NGF is important for the development, differentiation, and survival of variety of neuronal and non-neuronal cells. Its action is mediated by binding two distinct receptors, the high affinity p140 and low affinity p75.
Numéro de catalogue: (BOSSBS-3503R-CY3)

Fournisseur:  Bioss
Description:   Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11070R-A680)

Fournisseur:  Bioss
Description:   The amphoterin-induced gene and ORF (AMIGO) family of proteins consists of AMIGO-1, AMIGO-2 and AMIGO-3. All three members are single pass type I membrane proteins that contain several leucine-rich repeats, one IgG domain, and a transmembrane domain. The AMIGO proteins are specifically expressed on fiber tracts of neuronal tissues and participate in their formation. The AMIGO proteins can form complexes with each other, but can also bind itself. AMIGO-1, also designated Alivin-2, promotes growth and fasciculation of neurites and plays a role in myelination and fasciculation of developing neural axons. In cerebellar neurons, AMIGO-2 (Alivin-1) is crucial for depolarisation-dependent survival. Similar to AMIGO-1 and AMIGO-2, AMIGO-3 (Alivin-3) plays a role in homophilic and/or heterophilic cell-cell interaction and signal transduction.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-11166R)

Fournisseur:  Bioss
Description:   Sortilin-related receptor, also known as Sorting protein-related receptor containing LDLR class A (SorLA), is a Type I membrane protein that may be involved in cell-cell interaction. SorLA, a single transmembrane receptor, binds LDL (the main cholesterol-carrying lipoprotein of plasma) and transports it into cells by endocytosis. SorLA is synthesized as a proreceptor which is processed to the mature form by a furin-like propeptidase. It can also bind to RAP, receptor-associated protein. SorLa is a multifunctional endocytis receptor important in lipoprotein and protease uptake. The N-terminal propeptide, which is removed, can be cleaved by furin or homologous proteases. Endogenous sorLA binds the neuropeptide head activator (HA) and is important for HA signaling and function. It is expressed mainly in brain (cerebral cortex, cerebellum and the occipital pole), but can also be found in liver, spinal cord, kidney, testis and pancreas.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12305R-CY7)

Fournisseur:  Bioss
Description:   In eukaryotic cells, the Golgi apparatus receives newly synthesized proteins from the endoplasmic reticulum (ER) and, after covalent modification, delivers them to their destination in the cell. For membrane-directed proteins this process is believed to be carried out via vesicular transport. Correct vesicular transport is determined by specific pairing of vesicle-associated SNAREs (v-SNAREs) with those on the target membrane (t-SNAREs). Unconventional SNARE in the ER 1, also known as USE1 or protein p31, is a 259 amino acid t-SNARE that forms a larger complex with ZW10, RINT-1 and Syntaxin 18. Upon Mg2+-AP treatment in the presence of NSF and ?SNAP, ZW10, RINT-1 and USE1 dissociate from Syntaxin 18. USE1 is a single-pass type IV membrane protein that is localized to the endoplasmic reticulum membrane. Three named isoforms exist for USE1 as a result of alternative splicing events.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-13322R)

Fournisseur:  Bioss
Description:   Glycosylation of asparagine residues in Asn-X-Ser/Thr motifs in proteins commonly occur in the lumen of the endoplasmic reticulum (ER). Glucosidase I catalyzes the first step in the N-linked oligosaccharide processing pathway. It specifically removes the distal alpha 1,2-linked glucose residue from the Glc3-Man9-GlcNAc2 oligosaccharide precursor. Glucosidase I contains a short cytosolic tail, a single pass transmembrane domain and a large C-terminal catalytic domain located on the luminal side of the ER. Mutations in the gene encoding Glucosidase I result in the congenital disorder glycosylation (CDG-IIb), which is characterized by generalized hypotonia, dysmorphic features, hepatomegaly, hypoventilation, feeding problems, seizures and death. Two point mutations in the Glucosidase I gene have been identified and result in amino acid substitutions, namely Arg486Thr and Phe652Leu, that affect polypeptide folding and active site formation.
UOM:  1 * 100 µl
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