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Single-use+Temperature+Sensor
Numéro de catalogue:
(BOEI234100-2)
Fournisseur:
BOEKEL SCIENTIFIC
Description:
Whether crosslinking DNA or RNA, conducting Northern, Southern dot or slot blot analysis or UV curing, the UV Crosslinker AH provides a safe, time-efficient solution with a controlled amount of ultraviolet radiation. The UV Crosslinker AH incorporates an adjustable height feature which gives true-to-life readings by keeping samples on the base of the chamber, at the same distance from the bulbs as the fixed UV sensor. Instead of building up samples to get them closer to the bulbs, it is possible simply to adjust the bulbs to get them closer to the sample. The microprocessor detects the exact energy of the bulbs and compensates accordingly.
UOM:
1 * 1 ST
Numéro de catalogue:
(PRSI5045)
Fournisseur:
ProSci Inc.
Description:
FNIP2 Antibody: FNIP2 is the second protein found to interact with folliculin, the product of the Birt-Hogg-Dube (BHD) gene. Folliculin is thought to act as a tumor suppressor as mutations or loss of heterozygosity in this gene are associated with BHD syndrome-related renal tumors. Folliculin and FNIP1, a protein that shares 49% identity to FNIP2, bind to AMPK, an important energy sensor in cells that negatively regulates the mammalian target of rapamycin (mTOR), a protein that is thought to be the master switch for cell growth and proliferation. FNIP1 and FNIP2 are able to form homo- and heteromeric multimers, suggesting these proteins may have a functional relationship.
UOM:
1 * 1 EA
Numéro de catalogue:
(466-0310)
Fournisseur:
Thermo Fisher Scientific
Description:
Électrode, autre, Capteur d'échantillon
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-1913R-A680)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Numéro de catalogue:
(EUTE01X001530)
Fournisseur:
EUTECH
Description:
Électrode, multi-paramètres
UOM:
1 * 1 ST
Fournisseur:
SI Analytics
Description:
Ces cellules de conductivité haut de gamme sont idéales pour la surveillance et le contrôle des installations, ainsi que pour l'examen de l'eau ultrapure dans les laboratoires de contrôle qualité.
Numéro de catalogue:
(BOSSBS-1913R-CY7)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1913R-A647)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1913R-A350)
Fournisseur:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
UOM:
1 * 100 µl
Fournisseur:
Cole-Parmer
Description:
Cost-effective control of resistive heating loads.
Numéro de catalogue:
(PRSI90-326)
Fournisseur:
ProSci Inc.
Description:
Zinc-alpha-2-glycoprotein (ZAG), first identified in the 1960s, derives its name from its precipitation from human plasma upon the addition of zinc salts. ZAG has since been found in secretory epithelial cells and in a range of body fluids. ZAG is identical to a lipid mobilizing factor isolated from the urine of patients with cancer cachexia and stimulates lipolysis in in vitro and in vivo experiments. Due to its expression in, and secretion from adipocytes, ZAG is considered an adipokine. Recently the clinical significance of ZAG has been clarified. ZAG expression in adipocytes is inversely related to fat mass, thus it is intimately involved in the maintenance of body weight in mice and humans. Epidemiological studies have uncovered an association between ZAG and plasma cholesterol. The non-synonymous single nucleotide polymorphism rs4215 in ZAG is associated with plasma cholesterol and obesity. Structurally ZAG possesses a class I major histocompatibility complex (MHC) protein fold. It is distinct from other members of this protein family in that it is soluble, rather than being anchored to plasma membranes, and it associates with prolactin inducible protein rather than beta2-microglobulin. Similar to peptide antigen-presenting class I MHC molecules, ZAG possesses an open apical groove between its alpha1 and alpha2 domain helices.
UOM:
1 * 1 EA
Fournisseur:
ATAGO
Description:
These salt meters utilise the electric conductivity method and require no reagent solutions. They feature a funnel-shaped sensor section which measures the salinity in a solution of soluble materials.
Numéro de catalogue:
(YSIA606589)
Fournisseur:
YSI (ENVIRONMENTAL PRODUCTS
Description:
Simple, accurate pH measurement in sensors designed for minimal maintenance in sampling, profiling, and long-term monitoring applications.
UOM:
1 * 1 ST
Numéro de catalogue:
(453-2109)
Fournisseur:
GESTIGKEIT HARRY
Description:
The micro-processor controlled ramp controller is a complex time/temperature control and this program is indefinitely stored by means of an EEPROM.
UOM:
1 * 1 ST
Numéro de catalogue:
(181-0581)
Fournisseur:
Welch by Gardner Denver
Description:
Precise vacuum control for evaporation and distillation of solvents and chemicals.
UOM:
1 * 1 ST
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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