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3-[(2-Nitrophenoxy)methyl]pyrrolidine+hydrochloride
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3-[(2-Nitrophenoxy)methyl]pyrrolidine+hydrochloride
Catalog Number:
(10289-326)
Supplier:
Bioss
Description:
Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP3 (dipeptidyl-peptidase 3), also known as DPPIII, is a zinc-exopeptidase that belongs to the peptidase M49 family. DPP3 localizes to the cytoplasm and is involved in intracellular protein catabolism. More specifically, DPP3 is an important enzyme involved in the degradation of enkephalins. An increase in the activity of DPP3 is implicated in ovarian and endometrial cancers.
Catalog Number:
(10288-664)
Supplier:
Bioss
Description:
Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP3 (dipeptidyl-peptidase 3), also known as DPPIII, is a zinc-exopeptidase that belongs to the peptidase M49 family. DPP3 localizes to the cytoplasm and is involved in intracellular protein catabolism. More specifically, DPP3 is an important enzyme involved in the degradation of enkephalins. An increase in the activity of DPP3 is implicated in ovarian and endometrial cancers.
Catalog Number:
(10288-668)
Supplier:
Bioss
Description:
Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP3 (dipeptidyl-peptidase 3), also known as DPPIII, is a zinc-exopeptidase that belongs to the peptidase M49 family. DPP3 localizes to the cytoplasm and is involved in intracellular protein catabolism. More specifically, DPP3 is an important enzyme involved in the degradation of enkephalins. An increase in the activity of DPP3 is implicated in ovarian and endometrial cancers.
Catalog Number:
(10293-654)
Supplier:
Bioss
Description:
The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.
Catalog Number:
(10363-866)
Supplier:
Bioss
Description:
Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.
Catalog Number:
(75935-230)
Supplier:
Rockland Immunochemical
Description:
SAP90/PSD-95-associated protein 1 (SAPAP1, also known as DLGAP1 or GKAP) is a member of a protein family whose members specifically interact with PSD-95/SAP90, a membrane-associated guanylate kinase localized at postsynaptic density (PSD) in neuronal cells. Like the other SAPAP proteins, SAPAP1 is thought to be an adaptor protein that also interacts with different synaptic scaffolding proteins, cytoskeletal and signaling components, such as focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2). SAPAP1 mRNA is targeted to cell bodies in a similar manner to SAPAP2 and -4, whereas SAPAP3 mRNA is detected mainly in cell bodies. SAPAP1 protein however, is targeted to the synapse and is not reliant on the synaptic localization of PSD-95 or the synaptic scaffolding molecule (S-SCAM).
Catalog Number:
(10363-862)
Supplier:
Bioss
Description:
Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.
Catalog Number:
(10257-620)
Supplier:
Bioss
Description:
Flagella and cillia are both membrane-bound projections from the cell surface that beat in distinctive patterns. Cilia are shorter and usually more profuse than flagella and contain a microtubule cytoskeleton, the ciliary axoneme, surrounded by a ciliary membrane. The ciliary membranes of all cilia hold specific receptors and ion channel proteins that initiate signaling pathways that regulate motility and/or link mechanical or chemical stimuli to intracellular transduction cascades regulating differentiation, migration and cell growth during development and in adulthood. KPL2, also known as SPEF2 (sperm flagellar 2), is a 1,822 amino acid protein that contains a calponin homology domain, three nuclear localization signals, a consensus P-loop and a proline-rich region. Required for correct axoneme develoment, KPL2 is predominantly expressed in cells with cilia or flagella. Four isoforms of KPL2 exists as a result of alternative splicing events.
Catalog Number:
(10288-670)
Supplier:
Bioss
Description:
Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP3 (dipeptidyl-peptidase 3), also known as DPPIII, is a zinc-exopeptidase that belongs to the peptidase M49 family. DPP3 localizes to the cytoplasm and is involved in intracellular protein catabolism. More specifically, DPP3 is an important enzyme involved in the degradation of enkephalins. An increase in the activity of DPP3 is implicated in ovarian and endometrial cancers.
Catalog Number:
(10302-508)
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.
Catalog Number:
(10423-336)
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:
Biotium
Description:
This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®594 is a deep red fluorescent dye (Ex/Em 593/614 nm). It yields the brightest conjugates among spectrally similar dyes, and has excellent photostability.
Supplier:
Biotium
Description:
This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.
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.
Catalog Number:
(76194-256)
Supplier:
Prosci
Description:
Recognizes a protein of 40kDa, identified as CD7, 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.
Catalog Number:
(76194-252)
Supplier:
Prosci
Description:
Recognizes a protein of 40kDa, 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.
Catalog Number:
(10302-340)
Supplier:
Bioss
Description:
RUSC1 is a 902 amino acid protein that contains a RUN domain and a SH3 domain. RUSC1’s RUN domain is necessary for NGF induced nuclear redistribution. RUSC1 is a putative signaling adapter which may play a role in neuronal differentiation. RUSC1 seems to be involved in signaling pathways that are regulated by the prolonged activation of MAPK. RUSC2 (RUN and SH3 domain containing 2), also known as Iporin, is a 1,516 amino acid cytoplasmic protein that is widely expressed, with highest levels in brain and testis. The RUN domain of RUSC2 is required for interaction with Rab 1A, Rab 1B and GM130. It is thought that RUSC2 may possibly function as a connector between endoplasmic reticulum (ER) derived vesicle targets triggered by the Rab 1 GTPases and a signaling pathway regulated by molecules containing SH3 and/or poly-proline regions. RUSC2 also consists of a SH3 domain, suggesting a role in protein-protein interactions.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
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