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Update to Avantor’s response to the coronavirus (COVID-19) pandemic

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D-(+)-Proline


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Supplier:  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).

Supplier:  Bioss
Description:   The heredity chronic granulomatous disease (CGF) has been linked to mutations in p47-phox and p67-phox. The cytosolic proteins p47-phox and p67-phox, also designated neutrophil cytosol factor (NCF)1 and NCF2, respectively, are required for activation of the superoxide-producing NADPH oxidase in neutrophils and other phagocytic cells. During activation of the NADPH oxidase, p47-phox and p67-phox migrate to the plasma membrane where they associate with cytochrome b558 and the small G protein Rac to form the functional enzyme complex. Both p47-phox and p67-phox contain two Src homology 3 (SH3) domains. The C-terminal SH3 domain of p67-phox has been shown to interact with the proline-rich domain of p47-phox, suggesting that p47-phox may faciliate the transport of p67-phox to the membrane.
Supplier:  Bioss
Description:   The Src homology 3 (SH3) domain is a highly conserved 60 amino acid protein domain that is organized into a beta-barrel fold consisting of five or six beta strands arranged as two tightly packed anti-parallel beta sheets. This domain is found in proteins that mediate assembly of specific protein complexes and interact with other proteins, specifically recognizing proline-rich regions. BAIAP2L2 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2) is a 529 amino acid protein containing an SH3 domain, suggesting that it may function as an adaptor protein. BAIAP2L2 also contains an IMD (IRSp53/MIM) domain, which enables the protein to bind to and bundle Actin filaments, as well as bind to membranes and interact with Rac GTPase. There are two named isoforms of BAIAP2L2 which are produced as a result of alternative splicing events.

Supplier:  Bioss
Description:   The Src homology 3 (SH3) domain is a highly conserved 60 amino acid protein domain that is organized into a beta-barrel fold consisting of five or six beta strands arranged as two tightly packed anti-parallel beta sheets. This domain is found in proteins that mediate assembly of specific protein complexes and interact with other proteins, specifically recognizing proline-rich regions. BAIAP2L2 (Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2) is a 529 amino acid protein containing an SH3 domain, suggesting that it may function as an adaptor protein. BAIAP2L2 also contains an IMD (IRSp53/MIM) domain, which enables the protein to bind to and bundle Actin filaments, as well as bind to membranes and interact with Rac GTPase. There are two named isoforms of BAIAP2L2 which are produced as a result of alternative splicing events.

Supplier:  Bioss
Description:   Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK signaling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins (5). Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterization suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
Supplier:  Biotium
Description:   This antibody recognizes a protein of 40 kDa, identified as CD7 (Workshop IV; Code T155). CD7 is a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®647 is a far-red fluorescent dye (Ex/Em 650/665 nm) with excellent brightness. It also is compatible with super-resolution imaging by STORM.
Supplier:  Bioss
Description:   Polyglutamine(Q) tract binding protein-1 (PQBP-1) is a transcription repressor that associates with polyglutamine tract-containing transcription regulators and causative genes for neurodegenerative disorders. Hepta- and di-amino acid repeat sequences rich in polar residues are essential for PQBP-1 to interact with polyglutamine tract-containing proteins (i.e. huntingtin, androgen receptor and Brain-2). PQBP-1 contains a WWP/WW domain that binds proline-rich motifs and a C2 domain that can influence Ca2+-dependent phospholipid signaling. PQBP-1 localizes to the nucleus and is present in neurons throughout the brain, with abundant levels in hippocampus, cerebellar cortex and olfactory bulb. The human PQBP-1 gene maps to chromosome Xp11.23.

Supplier:  Bioss
Description:   Polyglutamine(Q) tract binding protein-1 (PQBP-1) is a transcription repressor that associates with polyglutamine tract-containing transcription regulators and causative genes for neurodegenerative disorders. Hepta- and di-amino acid repeat sequences rich in polar residues are essential for PQBP-1 to interact with polyglutamine tract-containing proteins (i.e. huntingtin, androgen receptor and Brain-2). PQBP-1 contains a WWP/WW domain that binds proline-rich motifs and a C2 domain that can influence Ca2+-dependent phospholipid signaling. PQBP-1 localizes to the nucleus and is present in neurons throughout the brain, with abundant levels in hippocampus, cerebellar cortex and olfactory bulb. The human PQBP-1 gene maps to chromosome Xp11.23.

Supplier:  Bioss
Description:   Polyglutamine(Q) tract binding protein-1 (PQBP-1) is a transcription repressor that associates with polyglutamine tract-containing transcription regulators and causative genes for neurodegenerative disorders. Hepta- and di-amino acid repeat sequences rich in polar residues are essential for PQBP-1 to interact with polyglutamine tract-containing proteins (i.e. huntingtin, androgen receptor and Brain-2). PQBP-1 contains a WWP/WW domain that binds proline-rich motifs and a C2 domain that can influence Ca2+-dependent phospholipid signaling. PQBP-1 localizes to the nucleus and is present in neurons throughout the brain, with abundant levels in hippocampus, cerebellar cortex and olfactory bulb. The human PQBP-1 gene maps to chromosome Xp11.23.
Supplier:  Bioss
Description:   Polyglutamine(Q) tract binding protein-1 (PQBP-1) is a transcription repressor that associates with polyglutamine tract-containing transcription regulators and causative genes for neurodegenerative disorders. Hepta- and di-amino acid repeat sequences rich in polar residues are essential for PQBP-1 to interact with polyglutamine tract-containing proteins (i.e. huntingtin, androgen receptor and Brain-2). PQBP-1 contains a WWP/WW domain that binds proline-rich motifs and a C2 domain that can influence Ca2+-dependent phospholipid signaling. PQBP-1 localizes to the nucleus and is present in neurons throughout the brain, with abundant levels in hippocampus, cerebellar cortex and olfactory bulb. The human PQBP-1 gene maps to chromosome Xp11.23.
Catalog Number: (10254-106)

Supplier:  Bioss
Description:   RIMS-binding proteins (RIM-BPs) serve as adaptors during vesicle fusion and release by forming links between synaptic-vesicle fusion apparatuses and calcium channels. Specifically, RIM-BP2 (RIMS binding protein 2), also known as RBP2, is a 1,052 amino acid protein that links L-type Ca++ CP Alpha1D, N-type Ca++ CP Alpha1B, Rim1 and Rim2 during synaptic transmission. RIM-BP2 contains three fibronectin type-III domains and three SH3 domains, which are used to mediate binding to a proline-rich motifs. Existing as three alternatively spliced isoforms, RIM-BP2 is encoded by a gene that maps to human chromosome 12q24.33 and mouse chromosome 5 G1.3.
Supplier:  Bioss
Description:   Shootin1 is a 631 amino acid protein that belongs to the shootin family. The shootin1 protein contains three coiled-coil domains, a proline-rich region and interacts with RUFY3. Shootin1 is involved in the generation of internal asymmetric signals required for neuronal polarization. The shootin1 protein acts upstream of PI3K (phosphoinositide 3-kinase), by being required for spatially localized PI3K activity. By accumulating asymmetrically in a single neurite before polarization, shootin1 leads to axon induction for polarization, additionally the absence of shootin1 from the nascent axon's siblings by competition prevents the formation of surplus axons. Existing as seven alternatively spliced isoforms, the shootin1 gene is conserved in chimpanzee, dog, mouse, rat, chicken and zebrafish, and maps to human chromosome 10q25.3.

Supplier:  Bioss
Description:   RIMS-binding proteins (RIM-BPs) serve as adaptors during vesicle fusion and release by forming links between synaptic-vesicle fusion apparatuses and calcium channels. Specifically, RIM-BP2 (RIMS binding protein 2), also known as RBP2, is a 1,052 amino acid protein that links L-type Ca++ CP Alpha1D, N-type Ca++ CP Alpha1B, Rim1 and Rim2 during synaptic transmission. RIM-BP2 contains three fibronectin type-III domains and three SH3 domains, which are used to mediate binding to a proline-rich motifs. Existing as three alternatively spliced isoforms, RIM-BP2 is encoded by a gene that maps to human chromosome 12q24.33 and mouse chromosome 5 G1.3.

Supplier:  Bioss
Description:   The fidelity of protein synthesis requires efficient discrimination of amino acid substrates by aminoacyl-tRNA synthetases. Aminoacyl-tRNA synthetases function to catalyze the aminoacylation of tRNAs by their corresponding amino acids, thus linking amino acids with tRNA-contained nucleotide triplets. ProRS (Prolyl-tRNA synthetase), also known as EPRS, EARS, PARS, QARS, QPRS, PIG32 or GLUPRORS, is a 1,512 amino acid protein that contains three WHEP-TRS domains and belongs to both the class-I and class-II aminoacyl-tRNA synthetase family. Functioning as a component of the multisynthase complex, ProRS uses ATP to catalyze the conversion of L-glutamate and tRNA(Glu) to L-glutamyl-tRNA(Glu), as well as the conversion of L-proline and tRNA(Pro) to L-prolyl-tRNA(Pro).

Supplier:  Bioss
Description:   Expressed mainly in breast, thymus, prostate, fetal liver, colon, placenta, pancreas, small intestine, spinal cord, kidney, and bone marrow and to a lesser extent in many other tissues. Isoform 2 is primarily expressed in skeletal muscle.

Supplier:  Bioss
Description:   Expressed mainly in breast, thymus, prostate, fetal liver, colon, placenta, pancreas, small intestine, spinal cord, kidney, and bone marrow and to a lesser extent in many other tissues. Isoform 2 is primarily expressed in skeletal muscle.
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