"Weight Sets"

Supplier: ZWIEBEL

These masses are intended for use calibrating of weights of a lower accuracy class and for use with weighing instruments of medium accuracy class III and and ordinary accuracy class IIII.

Supplier: Industrial Physics

Replacement weights for drying time recorder option, set of 6 pieces

Supplier: VWR Collection

Used in combination with contact plates, the contact weight enables the standardisation of microbiological surface control between operators. It applies the same constant pressure for a pre-set time on a contact plate. This ensures results are directly comparable. The contact weight meets the ISO 18593 standard, and has a sterilisable stainless steel base and pull-out digital timer.

Supplier: INTERSCIENCE

Gravimetric dilutor, Tube weights, Ø 6 mm

Supplier: INTERSCIENCE

Slangepumpe, Dispensing assembly, with a set of silicone tubings inner Ø 8 mm, GL45 screw cap, tube weight, nozzle, filter

Supplier: Rockland Immunochemicals

Lambda phage consists of a virus particle including a head (also known as a capsid), a tail and tail fibres. The head contains the phage's double-stranded circular DNA genome. The phage particle recognises and binds to its host E.coli causing DNA in the head of the phage to be ejected through the tail into the cytoplasm of the bacterial cell. Lambda phage DNA is commonly used as a DNA molecular weight marker. Digestion of the lambda phage genome with HindIII produces a set of 8 fragments consisting of 125, 560, 2000, 2300, 4300, 9400, and 23000 base pairs.

Supplier: VWR Collection

Complete communication kit with i-Weight software to connect a balance to a computer. Enables data collection, statistics, graphs and exports results to Excel. Functions: Piece counting, Density, Peak hold, Limits set. OS: Windows 7, 8, 10 (32&64). Note not suitable for use with moisture analysers

Supplier: Heidolph Scientific Products

From a unique, very wide speed range (1 to 32 rpm) to the timer (1 min to 999 h 59 min) to an integrated RS 232 interface, the Hei-SHAKE Salto Core has all core functions required for optimum processing of samples that tend to sedimentation. The maximum permissible weight is 30 kg, so that samples with a high solid content can be properly mixed (DIN 19529). Since this device sets large forces in motion, it is equipped with an emergency stop switch for your safety.

Supplier: VARIAN

Using these mixed columns you can eliminate mismatched column sets and spurious peaks for more reliable results. Every column contains a mixture of individual pore size materials, accurately blended to cover a specified broad range of molecular weight with a linear calibration to eliminate column mismatch. Simply add extra columns for even greater resolution.

Supplier: Spectrum Laboratories

Standardklemme
PP, autoklaverbare
Kun til regenererede cellulosemembraner
Da den er lettere end vand, bruges den normalt i kombination med fjederklemme
Vælg en klemme som er 4-10 mm større end den flade diameter på membranen

Supplier: SenseAnywhere

The SenseAnywhere AiroSensor 20-20-41 with Magnetic Door Contact Set is the ultimate solution to your refrigeration and freezer challenges!

Supplier: Merck Millipore (Novagen)

Molecular size markers for routine use in plasmid cloning, the Perfect DNA™ markers contain sets of DNA species having convenient, easy-to-remember sizes for agarose gel analysis. The markers have uniform band intensities except for the indicated reference bands, which are useful for instant band identification.

Supplier: ProSci Inc.

Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. SIGLEC12 is a member of the SIGLEC3-like subfamily of SIGLECs. SIGLEC12, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor.Western blots using four different antibodies against four unique regions of this protein target confirm the same apparent molecular weight in our tests.Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. This gene encodes a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains, and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. The encoded protein, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor. This gene is located in a cluster with other SIGLEC3-like genes on 19q13.4. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene.

Supplier: Amarell

Hydrometers with scale paper, colour code and type designation, weighted body, with (and without) thermometer inside the hydrometer body, round capillary, mercury filling suitable for government verification.

Supplier: ProSci Inc.

Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. SIGLEC12 is a member of the SIGLEC3-like subfamily of SIGLECs. SIGLEC12, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor.Western blots using four different antibodies against four unique regions of this protein target confirm the same apparent molecular weight in our tests.Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. This gene encodes a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains, and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. The encoded protein, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor. This gene is located in a cluster with other SIGLEC3-like genes on 19q13.4. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene.

Supplier: ProSci Inc.

Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. SIGLEC12 is a member of the SIGLEC3-like subfamily of SIGLECs. SIGLEC12, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor.Western blots using four different antibodies against four unique regions of this protein target confirm the same apparent molecular weight in our tests.Sialic acid-binding immunoglobulin-like lectins (SIGLECs) are a family of cell surface proteins belonging to the immunoglobulin superfamily. They mediate protein-carbohydrate interactions by selectively binding to different sialic acid moieties present on glycolipids and glycoproteins. This gene encodes a member of the SIGLEC3-like subfamily of SIGLECs. Members of this subfamily are characterized by an extracellular V-set immunoglobulin-like domain followed by two C2-set immunoglobulin-like domains, and the cytoplasmic tyrosine-based motifs ITIM and SLAM-like. The encoded protein, upon tyrosine phosphorylation, has been shown to recruit the Src homology 2 domain-containing protein-tyrosine phosphatases SHP1 and SHP2. It has been suggested that the protein is involved in the negative regulation of macrophage signaling by functioning as an inhibitory receptor. This gene is located in a cluster with other SIGLEC3-like genes on 19q13.4. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene.