Supplier: ASSAY TECHNOLOGY MS

ANESTHETIC GASES HALOGENATED

Supplier: ARBOR ASSAYS MS

ELISA KIT DNA DAMAGE

Supplier: ASSAY TECHNOLOGY MS

MONITOR 566 ORGANIC VAPOR 4CHEMICAL PK5

Supplier: ASSAY TECHNOLOGY MS

MONITOR 566 ORGANIC VAPOR 1CHEMICAL PK5

Supplier: ARBOR ASSAYS MS

THIOL DETECTION SYSTEM FLUOR RGT 500UG

Supplier: ARBOR ASSAYS MS

KIT ELISA CORTICOSTRONE CHEMILUMN 1PLATE

Supplier: ARBOR ASSAYS MS

KIT SERUM CREATININE DETECTION 2 PLATE

Supplier: ASSAY TECHNOLOGY MS

MONITOR 571 ALDEHYDE 1 ANALYTE PREPAID

Supplier: ARBOR ASSAYS MS

ELISA KIT 2 3-CYCLIC GAMP 5 PLATE

Supplier: ARBOR ASSAYS MS

PLATE GOAT ANTI-RABBIT IGG COATED

Supplier: ASSAY BIOTECHNOLOGY CO. INC MS

ANTIBODY MYOSIN REGULATORY LIGHT CHAIN 2

Supplier: ARBOR ASSAYS MS

PLATE 96 WELL BLACK HALF AREA

Supplier: ARBOR ASSAYS MS

KIT 2 3-CYCLIC GAM DIRECT ELA ONE PLATE

Supplier: G-Biosciences

KIT SSA ELISA 0.094 NG/ML 96 WELL PLATE

Supplier: ARBOR ASSAYS MS

SOLVENT DRY DMSO 4ML STORE AT ROOM TEMP

Supplier: MP Biomedicals

Dimethyl Sulfoxide is ideal for use as a cryoprotectant. Also used in chemical reactions, in polymerase chain reactions (PCR) as a PCR cosolvent to help improve yields, especially in long PCR, and as a cryoprotectant vitrification agent for the preservation of cells, tissues and organs. DMSO is used in cell freezing media to protect cells from ice crystal-induced mechanical injury. It is used for frozen storage of primary, sub-cultured, and recombinant heteroploid and hybridoma cell lines, embryonic stem cells (ESC), and hematopoietic stem cells. DMSO is frequently used in the combinations with BSA or fetal bovine serum (FBS). Used to enhance dermal absorption of many chemicals. A solvent for many organic and inorganic compounds including fats, carbohydrates, dyes, resins, and polymers. Used in antifreeze or hydraulic fluids. A cryopreservative for cell cultures. Used in the oxidation of thiols and disulfides to sulfonic acids.

Dimethyl sulfoxide (DMSO) is a highly polar aprotic organic reagent that has exceptional solvent properties for organic and inorganic chemicals

Physical Apppearance: Liquid
Viscosity: 1.1 centipoises (27 °C)
Vapor Density: 2.7 (vs air)
Vapor Pressure: 0.55 hPa at 20 °C, 0.42 mmHg (20 °C)
Refractive Index: n20/D 1.479(lit.)
Solubility: Soluble in water (1 mL DMSO + 1 mL H2O), methanol, acetone, ether, benzene, chloroform

Supplier: Prosci

Programmed cell death 1 ligand 2 (PD-L2), also known as butyrophilin B7-DC or PDCD1 ligand 2, belongs to the member of B7 family which can regulate the activation and tolerance of T cells. PD-L2 is one ligand for Programmed cell death 1(PD-1), and the other is PD-L1. These two ligands shares 34% aa sequence identity. Mouse PD-L2 gene encodes a 273 amino acids (aa) protein with a putative 19 aa signal peptide, a 201 aa extracellular region , a 21 aa transmembrane domain and a 32 aa cytoplasmic region. The mouse PD-L2 gene is highly expressed in heart, placenta, pancreas, lung and liver while expressed weakly in spleen, lymph nodes and thymus. Besides, the expression of PD-L2 gene can be induced on dendritic cells grown from peripheral blood mononuclear cells under CSF2 and IL4/interleukin-4 treatment, and up-regulated by IFNG/IFN-gamma stimulation in monocytes. PD-L2 usually functions in a PDCD1-independent manner and is involved in regulating costimulatory signal which is essential for T-cell proliferation and IFNG production. Recent studies demonstrate that the expression of PD-L2 on the tumor cells promotes CD8 T cell–mediated rejection of tumor cells, at both the induction and effector phase of antitumor immunity. Moreover, PD-L2 binds to PD-1 cells and enhances T cell killing in a PD-1–independent mechanism.

Supplier: ASSAY CELL TECHNOLOGIES INC MS

GLOVE EXAM LATEX CURAD PF MD 21LB CS1000

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: Promega Corporation

The PureYield RNA Midiprep System isolates intact, pure total RNA from essentially any sample type for use in a wide range of applications.

Supplier: Biotium

Biotium’s DNA Gel Extraction Kit is a silica-gel, spin column based DNA extraction kit.

Supplier: Genetex

The 90kDa molecular chaperone family comprises several proteins including the 90kDa heat shock protein, Hsp90 and the 94kDa glucose regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and hsp90s which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90a is 85% and 90% homologous to that of Hsp90s respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N terminal and C terminal regions which have been shown to contain independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steriod receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways.

Supplier: Genetex

The 90kDa molecular chaperone family comprises several proteins including the 90kDa heat shock protein, Hsp90 and the 94kDa glucose regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and hsp90s which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90a is 85% and 90% homologous to that of Hsp90s respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N terminal and C terminal regions which have been shown to contain independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steriod receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways.

Supplier: Cytiva

For rapid buffer exchange/desalting of PCR products and other DNAs in a volume of 10 to 100 μl using spin column chromatography.

Supplier: Prosci

Reacts with a protein of 57kDa, identified as the L1 protein of human papilloma virus type 16 (HPV-16). Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on the basement membrane to provide initial virion attachment to target cells. Basement membrane is exposed only after epithelium trauma. Additionally, the alpha6 integrin complexed with either beta1 or beta4 integrin has been proposed to act as a coreceptor recognized by L1. Once attached, integrin complexed with beta4 integrin has been proposed to act as a coreceptor recognized by L1. Once attached, the virion enters the host cell via clathrin-mediated endocytosis and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2. [UniProt]

The antibody reacts very strongly with formalin-fixed, paraffin-embedded tissues containing HPV-16 or -33; very weak reactions were occasionally observed with biopsy specimens or smears containing HPV-6 or HPV-11. It cross-reacts with HPV37.

Supplier: Prosci

Programmed Death-1 (PD-1), firstly cloned from mouse T cell hybridoma 2B4.11, is one member of CD28/CTLA-4 superfamily. PD-1 belongs to type I transmembrane protein and acts as an important immunosuppressive molecule. This family also include members of CD28, CTLA-4 and ICOS.The mouse Programmed Death-1 protein, encoded by PD-1 gene, comprises four parts including a putative 20 aa signal peptide, a 149 aa extracellular region, a 21 aa transmembrane domain and a 98 aa cytoplasmic region. The cytoplamsic tail of PD-1 contains two structural motifs, an immunoreceptor tyrosine-based inhibitory motif (ITIM) and an immunoreceptor tyrosine-based switch motif (ITSM) formed by two tyrosine residues which make the difference in PD-1 signal mediating. Mouse PD-1 is expressed in thymus and shares about 69% aa sequence identity with human PD-1. Recently, programmed death-1 (PD-1) with its ligands, programmed death ligand B7H1 (PD-L1) and B7DC (PD-L2), was found to regulate T-cell activation and tolerance, upon ligand binding, inhibiting T-cell effector functions in an antigen-specific manner. PD-1 gene knocked out mice would induce some autoimmune diseases, which suggests that PD-1 acts as a co-inhibitory molecule actively participating in maintaining peripheral tolerance. Thus, PD-1 may be a useful target for the immunologic therapy of carcinoma,infection,autoimmune diseases as well as organ transplantation.

Supplier: Cytiva

illustra™ MicroSpin™ S-300 HR columns designed for rapid purification of PCR products (>100 bp) from unincorporated primers (<20-mers) and nucleotides using spin-column chromatography.

Supplier: Promega Corporation

The QuantiFluor ssDNA System contains a fluorescent dye that enables sensitive quantitation of small amounts of single-stranded (ssDNA) in solution.

Supplier: Genetex

The serum amyloid A family comprises a number of differentially expressed apolipoproteins, acute-phase SAA1 and SAA2, the former being the major component in plasma and constitutive SAAs. Although the liver is the primary site of synthesis of both SAA types extrahepatic production has been reported. The in vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed its importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations; SAA rises earlier and more sharply than CRP. Recently, a broader view of SAA expression and function has been emerging. Expression studies show production of SAA proteins in histologically normal, atherosclerotic, Alzheimer, inflammatory, and tumour tissues. SAA has been found to have binding sites for high density lipoproteins, calcium, laminin, and heparin/heparin sulphate. Also adhesion motifs were identified and new functions affecting cell adhesion, migration, proliferation, and aggregation were discovered. These findings emphasize the importance of SAA in various physiological and pathological processes including inflammation, atherosclerosis, thrombosis, AA-amyloidosis, rheumatoid arthritis, and neoplasia. SAA has also a number of immunomodulatory roles, it can induce chemotaxis and adhesion molecule expression, has cytokine-like properties and can promote the upregulation of metalloproteinases. It enhances the binding of high density lipoprotein to macrophages and thus helps in the delivery of lipids to sites of injury for use in tissue repair, it is thus thought to be an integral part of the disease process.

Supplier: Genetex

BRCA1 (breast and ovarian cancer susceptibility protein 1) is a RING finger protein containing a BRCT domain. BRCA1 exists as a heterodimer with 22 possible isoforms. The full length protein has a reported molecular weight of 208 kD. BRCA1 localizes to the mitotic spindle microtubules, centriole walls, pericentriolar fibers at centrosomes. Unphosphorylated BRCA1 localizes on chromosomes from metaphase through telophase; phosphorylated BRCA1 resides in inner chromosomal structure, centrosome, cleavage furrow during prophase through telophase, and relocalizes to the perinuclear region when cells are subjected to IR or UV radiation in S phase. BRCA1 acts as a tumor suppressor and can function as a secreted growth inhibitory protein, participate in transcription coupled repair of oxidative DNA damage, X-chromosome inactivation, and can function as a E3 ubiquitin ligase. BRCA1 can be transcriptionally downregulated by Ets-2, Brg-1, and Hmga-1. BRCA1 can be modified by glycosylation, ubiquitination and phosphorylation by CDK4, ATM/ATR, cdk2, and hChk2. The BRCA1 protein has been reported to interact with RNA polymerase II holoenzyme and BARD1. BRCA1 contains at least two nuclear localization signals and is proposed to be a tumor suppressor protein. It is a serine phosphoprotein that undergoes hyperphosphorylation during late G1 and S phases of the cell cycle and is transiently dephosphorylated early after M phase. BRCA1 protein alters in a qualitative and quantitative manner during cell cycle progression. The amount of BRCA1 protein is highest during S phase and remains elevated toward G2 / M, before it declines in early G1 phase. Inherited loss of BRCA1 function confers an increased susceptibility for both breast and ovarian cancer.