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Catalog Number: (77149-664)

Supplier:  AMBEED, INC
Description:   (S)-N-Ethylpyrrolidine-2-carboxamide hydrochloride, Purity: 97%, CAS Number: 58107-62-3, Appearance: White to yellow powder or crystals, Storage: Inert atmosphere, Room Temperature, Size: 10g
Catalog Number: (103409-026)

Supplier:  Novus Biologicals
Description:   The PRODH Antibody from Novus Biologicals is a goat polyclonal antibody to PRODH. This antibody reacts with human. The PRODH Antibody has been validated for the following applications: Western Blot, Peptide ELISA.

Supplier:  Bioss
Description:   Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform beta-1B interferes with isoform beta-1A resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
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®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.
Supplier:  Biotium
Description:   This antibody recognizes a protein of 40 kDa, identified as CD7 (also known as gp40, Leu9). 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®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.
Supplier:  Bioss
Description:   This gene encodes coagulation factor XII which circulates in blood as a zymogen. This single chain zymogen is converted to a two-chain serine protease with an heavy chain (alpha-factor XIIa) and a light chain. The heavy chain contains two fibronectin-type domains, two epidermal growth factor (EGF)-like domains, a kringle domain and a proline-rich domain, whereas the light chain contains only a catalytic domain. On activation, further cleavages takes place in the heavy chain, resulting in the production of beta-factor XIIa light chain and the alpha-factor XIIa light chain becomes beta-factor XIIa heavy chain. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. The active factor XIIa participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. It activates coagulation factors VII and XI. Defects in this gene do not cause any clinical symptoms and the sole effect is that whole-blood clotting time is prolonged.
Catalog Number: (10271-026)

Supplier:  Bioss
Description:   In Drosophila, neuronal cell fate decisions are directed by NUMB, a signaling adapter protein with two protein-protein interaction domains, namely a phosphotyrosine-binding domain and a proline-rich SH3-binding region (PRR). The mammalian NUMB homolog plays a role in the determination of cell fate during development and binds with a variety of proteins, including Eps15, LNX1 and Notch 1. NumbL (NUMB-like protein), also known as Numb-R, NBL, CAG3A, CTG3a, NUMBLIKE or TNRC23, is a 609 amino acid cytoplasmic protein that, like NUMB, is thought to play a role in cell fate. Expressed at high levels in developing brain tissue, NumbL contains one PID (phosphotyrosine interaction domain) and plays an important role in neuronal differentiation, possibly associating with Eps15 and Notch 1. In mice, deletion of the NumbL gene is associated with early embryonic death, suggesting an essential role for NumbL in early development.
Catalog Number: (10292-890)

Supplier:  Bioss
Description:   A gene on chromosome 20q13.1 encodes Eya2 (eyes absent). EYA2 is one of four members of the eyes absent family. A 271 amino acid domain at the carboxy-terminal is highly conserved amongst the members of the eyes absent family, while the PST (proline-serive-threonin)-rich amino-terminal is highly divergent. EYA2 is expressed relatively late in development in the cytoplasm of extensor tendons and ligaments of the phalangeal elements of the limb, cranial placodes, branchial arches, central nervous system, and the developing eye. Pax3 induces the expression of Eya2 in a cascade that is necessary and sufficient for myogenesis. EYA2, like EYA1, acts as a transcriptional activator in connective tissue patterning through its PST domain, which functions as a transactivation domain. EYA2 is translocated to the nucleus by Six proteins, which interact through their domain and homeodomain with EYA2. EYA2 carboxy-terminal interacts with the G Alpha z and G Alphai 2 proteins. This interaction prevents Six proteins from translocating EYA2 to the nucleus.

Supplier:  Bioss
Description:   A gene on chromosome 20q13.1 encodes Eya2 (eyes absent). EYA2 is one of four members of the eyes absent family. A 271 amino acid domain at the carboxy-terminal is highly conserved amongst the members of the eyes absent family, while the PST (proline-serive-threonin)-rich amino-terminal is highly divergent. EYA2 is expressed relatively late in development in the cytoplasm of extensor tendons and ligaments of the phalangeal elements of the limb, cranial placodes, branchial arches, central nervous system, and the developing eye. Pax3 induces the expression of Eya2 in a cascade that is necessary and sufficient for myogenesis. EYA2, like EYA1, acts as a transcriptional activator in connective tissue patterning through its PST domain, which functions as a transactivation domain. EYA2 is translocated to the nucleus by Six proteins, which interact through their domain and homeodomain with EYA2. EYA2 carboxy-terminal interacts with the G Alpha z and G Alphai 2 proteins. This interaction prevents Six proteins from translocating EYA2 to the nucleus.

Supplier:  Bioss
Description:   A gene on chromosome 20q13.1 encodes Eya2 (eyes absent). EYA2 is one of four members of the eyes absent family. A 271 amino acid domain at the carboxy-terminal is highly conserved amongst the members of the eyes absent family, while the PST (proline-serive-threonin)-rich amino-terminal is highly divergent. EYA2 is expressed relatively late in development in the cytoplasm of extensor tendons and ligaments of the phalangeal elements of the limb, cranial placodes, branchial arches, central nervous system, and the developing eye. Pax3 induces the expression of Eya2 in a cascade that is necessary and sufficient for myogenesis. EYA2, like EYA1, acts as a transcriptional activator in connective tissue patterning through its PST domain, which functions as a transactivation domain. EYA2 is translocated to the nucleus by Six proteins, which interact through their domain and homeodomain with EYA2. EYA2 carboxy-terminal interacts with the G Alpha z and G Alphai 2 proteins. This interaction prevents Six proteins from translocating EYA2 to the nucleus.

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. DPP10 (dipeptidyl-peptidase 10), also known as DPRP3 (dipeptidyl peptidase IV-related protein 3), DPL2 or DPPY, is a non-functional dipeptidyl peptidase which can bind to the potassium channels KV4.1 and KV4.2. It is a single-pass type II membrane protein expressed in spinal cord, adrenal glands, pancreas and brain tissues and may act as a modulator for cell surface expression and activity of KV4.1 and KV4.2.
Catalog Number: (10286-414)

Supplier:  Bioss
Description:   The protease enzyme Lethal Factor (LF) is one of the three proteins (LF, EF & PA) composing the anthrax toxin produced by Bacillus anthracis, a bacteria which can infect many mammalian species and that may be fatal. LF is not toxic by itself, but when associated with Protective Antigen (PA), can then gain entry to cells. Once inside the cell, LF then cleaves the N terminal of most dual specificity mitogen activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N terminal proline rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LF intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.
Catalog Number: (75932-304)

Supplier:  Rockland Immunochemical
Description:   The serine/threonine kinase Stk39 belongs to the STE20 family, a group of kinases that are known to interact with inflammation-related kinases (such as p38, JNK, NKCC1, PKC-theta, WNK and MLCK), and with transcription factor AP-1. The STE 20 family is involved in diverse biological phenomena, including cell differentiation, cell transformation/ proliferation, cytoskeleton rearrangement, and the regulation of ion transporters. STK39 contains an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain and is abundantly expressed in the brain. STK39 is activated in response to hypotonic stress, leading to phosphorylation of several cation-chloride-coupled co-transporters. The catalytically active kinase specifically activates the p38 MAP kinase pathway, and its interaction with p38 decreases upon cellular stress, suggesting that this kinase may serve as an intermediate in the response to cellular stress. Recent studies show that STK39 tend to be a novel candidate gene for autism and hypertension.
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®488A is a green fluorescent dye (Ex/Em 490/515 nm) with excellent brightness and photostability. The dye is minimally charged for less non-specific binding. CF®488A also is compatible with super-resolution imaging by TIRF.

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.
Catalog Number: (75793-504)

Supplier:  Prosci
Description:   Profilin (PFN1) is a ubiquitous small (12-15kDa) phosphoinositide and poly-L-proline binding protein that plays a role in signal transduction pathways and actin filament dynamics. There are two mammalian profilins with similar biochemical properties. Whereas profilin I appears to be highly expressed in most tissues except for skeletal muscle, profilin II is predominantly expressed in brain and at lower levels also in skeletal muscle, uterus and kidney. Profilin is a mainly cytosolic protein with higher concentrations in dynamic membrane areas like the leading edge and ruffling membranes. Profilin binding to PIP2 interferes with PIP2 hydrolysis by soluble phospholipase C-gamma, an inhibition that can be overcome by tyrosine phosphorylation of PLC-gamma. Besides actin monomer sequestration and stimulation of actin nucleotide exchange, profilin can also promote cellular actin filament growth. Profilin is involved in the actin dependent intracellular motility of cytopathogenic bacteria, the regulation of cell adhesion and possibly also in linking the actin cytoskeleton and endocytosis. Profilin has been found to associate with defined complexes containing proteins such as Arp2/3 or the Rho/Rac pathways constituents ROCK-II and HEM2/NAP1. Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18).
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