35791 Results for: "Capitol Vial Specimen Collection"

Supplier: Omega Bio-Tek

Isolates total RNA from blood samples stored in special preservation reagents and PAXgene tubes using spin columns.

Supplier: Thermo Fisher Scientific

Get premium performance and flexibility with the Orion™ Versa Star Pro™ Meter with pH and Conductivity Modules for simultaneous pH, conductivity, and temperature analysis.

Supplier: Cytiva

illustra™ MicroSpin™ S-400 HR columns designed for rapid purification of PCR products (>200 bp) from unincorporated primers (<32-mers) and nucleotides using spin-column chromatography.

Supplier: CREATIVE BIOARRAY MS

CELL_PRIMARY_KIDNEY_RAT_PROXIMAL_1_VIAL

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

The lymphocyte-specific kinase (Lck) is a cytoplasmic tyrosine kinase of the Src family expressed in T cells and natural killer (NK) cells. Genetic evidence in both mice and humans demonstrates that Lck kinase activity is critical for signaling mediated by the T cell receptor (TCR), which leads to normal T cell development and activation. Selective inhibition of Lck is expected to offer a new therapy for the treatment of T-cell-mediated autoimmune and inflammatory disease. AMG-47 is one of two optimized chemical compounds that has been shown to be extremely effective in vivo and in vitro in inhibiting Lck as well as a number of other receptor tyrosine kinases. In an anti-CD3/ IL-2 mouse model system AMG-47 has been shown to be effective in inhibiting the Lck mediated anti-inflammatory activity (ED50 11 mg/kg; 630nM) in vivo. In multiple other in vitro assays, AMG-47 exhibits subnanomolar inhibition against Lck, and low (10nM) inhibition against other hard to inhibit kinases such as KDR and SRC and MAPK alpha (p38alpha). Moreover at slightly higher doses but well under 10µM, AMG-47 effectively inhibits the JNK family of kinases including TYK2 at ~ 1.2µM.

Supplier: Adipogen

AT7519 is a potent inhibitor of several CDK family members. AT7519 showed potent antiproliferative activity (40-940nM) in a panel of human tumor cell lines, and the mechanism of action was shown here to be consistent with the inhibition of CDK1 and CDK2 in solid tumor cell lines. AT7519 caused cell cycle arrest followed by apoptosis in human tumor cells and inhibited tumor growth in human tumor xenograft models. Tumor regression was observed following twice daily dosing of AT7519 in the HCT116 and HT29 colon cancer xenograft models. Also it has been shown that the biological effects are linked to inhibition of CDKs in vivo and that AT7519 induces tumor cell apoptosis in these xenograft models. Moreover, AT7519 has an attractive biological profile and is well tolerated and effective making it a more plausible candidate for clinical development than previously available CDK inhibitors. In in vitro kinase assays AT7519 showed nanomolar levels of activity from 10 to 2400 for cyclins; only one other non-cyclin related kinase was inhibited at levels below 10µM (GSK3beta, 89nM), all others tested had IC(50)'s of greater than 10,000nM.

Supplier: CREATIVE BIOARRAY MS

CELL_RAT_SKELETAL_MUSCLE_ONE_FROZEN_VIAL

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Uncharged, hydrophobic, photostable fluorescent probe that strongly fluoresces bright red in hydrophobic (lipid-rich) environments, but is almost nonfluorescent in water. This lipophilic stain is commonly used for the detection of intracellular lipid droplets in cells such as adipocytes by fluorescence microscopy and flow cytometry. It has been shown to detect the exposure or formation of new hydrophobic surfaces induced by ligand binding to calmodulin, oligomerization of melittin, or unfolding of ovalbumin during early thermal denaturation. This product has been employed to stain cell structures, as well as to visualize and localize colloidal drug carriers. Has been used to stain lipophilic proteins that have been separated by SDS-PAGE electrophoresis or to detect sphingolipids on thin-layer chromatograms. The fluorescence is unaffected between pH 4.5 and 8.5 and may be used in dilute concentrations to investigate hydrophobic protein sites. Spectral properties: Intracellular fat vacuoles, filled with neutral lipids such as cholesterol, lipoproteins and triglycerides will fluoresce green (Abs/Em =485/525) while polar lipids, such as phospholipids, will fluoresce red (Abs/Em = 552/636 nm).

Supplier: Adipogen

Antagonizing the Chk1-mediated cell cycle checkpoints has emerged as an attractive target for anticancer therapy. If Chk1 activity is blocked, DNA-damaged or spindle-disrupted cells would exit cell cycle arrest before full repair and subsequently undergo mitotic catastrophe or cell death. Chk1 inhibitors consequently increase the therapeutic index of DNA-damaging or antimitotic agents as well. PF-0477736 is a selective, potent ATP-competitive Chk1 inhibitor, derived from PF-0394691, inhibits Chk1 (Ki, 0.49nM) and Chk2 (Ki, 47nM) in vitro. In tests, PF-0477736 was identified as a potent, selective ATP-competitive small-molecule inhibitor that inhibits Chk1 with a Ki of 0.49nM. PF-0477736 abrogates cell cycle arrest induced by DNA damage and enhances cytotoxicity of clinically important chemotherapeutic agents, including gemcitabine and carboplatin. In xenografts, PF-0477736 enhanced the antitumor activity of gemcitabine in a dose-dependent manner. PF-0477736 combinations were well tolerated with no exacerbation of side effects commonly associated with cytotoxic agents.

Supplier: Orflo

VALIDATION BEADS FOR MOXI FLOW (ONLY)

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4), a member of the highly conserved protein family of TLRs, which are specialised in the recognition of microbial components. In mice, defects in TLR4 result in LPS unresponsiveness. For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). This mechanism is believed to be generally true for LPS signaling. Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. Monophosphoryl Lipid A (MPLA) represents a detoxified derivative of Lipid A and constitutes an important adjuvant in prophylactic and therapeutic vaccines.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4), a member of the highly conserved protein family of TLRs, which are specialised in the recognition of microbial components. In mice, defects in TLR4 result in LPS unresponsiveness. For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). This mechanism is believed to be generally true for LPS signaling. Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. Monophosphoryl Lipid A (MPLA) represents a detoxified derivative of Lipid A and constitutes an important adjuvant in prophylactic and therapeutic vaccines.

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

KG-1

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Water soluble pH indicator used in the 6.8 (yellow) to 8.2 (red) range and frequently used in cell biology laboratories. Widely used as cell tissue culture pH marker. A small amount of phenol red added to the growth medium will have a pink-red color under normal conditions. Typically, 15 mg/l are used for cell culture. In the event of problems, waste products produced by dying cells or overgrowth of contaminants will cause a change in pH, leading to a change in indicator color. For example, a culture of relatively slowly dividing mammalian cells can be quickly overgrown by bacterial contamination. This usually results in an acidification of the medium, turning it yellow. The waste products produced by the mammalian cells themselves will slowly decrease the pH, gradually turning the solution orange and then yellow. This color change is an indication that even in the absence of contamination, the medium needs to be replaced. Shown to be a weak estrogen mimic (possible through inpurities), which can enhance the growth of cells that express the estrogen receptor in cell cultures. Might be useful as a differentiation factor.

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

LYMPHOBLAST SR

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

CELLS SW620

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

CELLS ASPC-1

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

CELLS REC-1

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

TT CELLS

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

CTLL-2 LYMPHOCYTES

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

HUMAN NEUROBLASTOMA

Supplier: Adipogen

Activation of cells by LPS is mediated by the Toll-like receptor 4 (TLR4). For optimal interaction with LPS, TLR4 requires association with myeloid differentiation protein 2 (MD-2). According to current consensus activation of TLR4 is preceded by the transfer of LPS to membrane-bound (m) or soluble (s) CD14 by LPS-binding protein (LBP). Re-form LPS and lipid A, but not S-form LPS, are capable of inducing TNF-alpha responses also in the absence of CD14. LPS, synthesized by most wild-type (WT) Gram-negative bacteria (S-form LPS), consists of three regions, the O-polysaccharide chain, which is made up of repeating oligosaccharide units, the core oligosaccharide and the lipid A, which harbors the endotoxic activity of the entire molecule. R-form LPS synthesized by the so-called rough (R) mutants of Gram-negative bacteria lacks the O-specific chain. Furthermore, the core-oligosaccharide may be present in different degrees of completion, depending on the class (Ra to Re) to which the mutant belongs. LPS are amphipathic molecules whose hydrophobicity decreases with increasing length of the sugar part. Based upon these differences, S- and R-form LPS show marked differences in the kinetics of their blood clearance and cellular uptake as well as in the ability to induce oxidative burst in human granulocytes and to activate the host complement system.

Supplier: Adipogen

Naturally occurring carnitine derivative formed by carnitine acetyltransferase during beta-oxidation of uneven chain fatty acids, with high affinity for muscular carnitine transferase. Increases cellular carnitine content, allowing free fatty acid transport into the mitochondria. Stimulates energy production in ischaemic muscles by increasing citric acid cycle flux and stimulating pyruvate dehydrogenase activity. Important for mitochondrial metabolism and energy regulation. Regulates the metabolism of both carbohydrates and lipids, leading to an increase of ATP generation. Selectively inhibits in vitro and ex vivo platelet-activating factor (PAF) synthesis from human neutrophils. Antioxidant. Shows free radical scavenging activity. Decreases the expression of inducible nitric oxide synthase (iNOS/NOS II) and NADPH-oxidase 4-mediated reactive oxygen species production in human umbilical vascular endothelial cells. Shows beneficial cardiovascular effects. Improves body weight, food intake, adiposity and insulin resistance in Type 2 diabetes. Stimulates endothelial nitric oxide (eNOS/NOS III) and increased NO production, via AMPK/Src-mediated signaling that leads to activation of PI3 kinase and Akt.

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

CELL LINE CA46

Supplier: AMERICAN TYPE CULTURE COLLECTION MS

CELLS HMEC-1 ENDOTHELIUM