Collagens
Collagen, Bovine Achilles tendon
For research use
INTACT GENOMICS INC ig 5-alpha Chemically Competent Cells (High Efficiency) 96 x 50µl (12 8-well strip)
Intact Genomics 5 alpha chemically competent E. coli cells are suitable for high efficiency transformation in a wide variety of applications such as cloning and sub-cloning. ig 5 alpha chemically competent cells are at least twice the transformation efficiency of the nearest competitor.Product Includes & Storage:ig 5 alpha Competent Cells: -80 ºCpUC19 control DNA: -20 ºCRecovery medium: 4 ºC
Sigma Aldrich Fine Chemicals Biosciences Collagen from rat tail ten
Collagens are abundantly present in vertebrates. 41 specific genes codes for 42 polypeptide chains and produce 27 collagen types. Collagens nbspare mainly present in the extracellular matrix. Collagen type I is abundantly present in mammals. Type IV collagen is an important structural protein of basement membranes. It is chemically and genetically different from stroma collagen types I and III and cartilage collagen type II.
Sigma Aldrich Fine Chemicals Biosciences sIL 6 Receptor alpha human
Interleukin-6 (IL-6) mediates its biological effects through the type I IL-6 receptor system that consists of two chains IL-6RÎ and gp130. The IL-6RÎ chain is the binding component specific to IL-6 while the gp130 only transmits signals of IL-6 when bound to IL-6RÎ. IL-6R has a role in various signaling cascades. The gp130 also can transmit signals from leukemia inhibitory factor (LIf) oncostatin M (OSM) ciliary neurotrophic factor (CNTf) interleukin-11 (IL-11) and cardiotrophin-1 (CT-1) in conjunction with other receptor subunits. The low-affinity binding site for IL-6 is composed of IL-6RÎ alone. IL-6RÎ is expressed in a wide range of cells including T cells fibroblasts and macrophages. Soluble IL-6RÎ which consists of only the extracellular domain of the IL-6RÎ chain acts as an agonist of IL-6 activity at low concentrations. Recombinant human sIL-6RÎ is a 37.6kDa protein consisting of the extracellular domain of the IL-6RÎ chain (339 amino acid residues).
Sigma Aldrich Fine Chemicals Biosciences Collagen from bovine achilles tendon powder, suitable for substrate for collagenase | 9007-34-5 | MFCD00130825 | 5G
Collagen from bovine achilles tendon powder, suitable for substrate for collagenase | 9007-34-5 | MFCD00130825 | 5G
Sigma Aldrich Fine Chemicals Biosciences Collagen Type IV from human cell culture | 9007-34-5 | MFCD00130825 | 1ml
Collagen Type IV from human cell culture | 9007-34-5 | MFCD00130825 | 1ml
Sigma Aldrich Fine Chemicals Biosciences Collagen from human placenta Bornstein and Traub Type IV, powder, BioReagent, suitable for cell culture | 9007-34-5 | MFCD00130825 | 5mg
Collagen from human placenta Bornstein and Traub Type IV, powder, BioReagent, suitable for cell culture | 9007-34-5 | MFCD00130825 | 5mg
Sigma Aldrich Fine Chemicals Biosciences Collagen from calf skin | 9007-34-5 | MFCD00130825 | 20ml
Collagen from calf skin | 9007-34-5 | MFCD00130825 | 20ml
Sigma Aldrich Fine Chemicals Biosciences Rat Tail Collagen Coating Solution (20 ML)
Rat Tail Collagen Coating Solution (20 ML)
Sigma Aldrich Fine Chemicals Biosciences Poly-L-ornithine solution, 27378-49-0, MFCD00286305, 50mL
Mol Wt 30,000-70,000, 0.01%, sterile-filtered, BioReagent, suitable for cell culture. Poly-L-ornithine is a positively charged synthetic amino acid polymer.
Sigma Aldrich Fine Chemicals Biosciences Collagen from rat tail Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture | 9007-34-5 | MFCD00130825 | 5MG
Collagen from rat tail Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture | 9007-34-5 | MFCD00130825 | 5MG
Sigma Aldrich Fine Chemicals Biosciences Collagen from rat tail | 9007-34-5 | MFCD00130825 | 25mg
Collagen from rat tail | 9007-34-5 | MFCD00130825 | 25mg
Sigma Aldrich Fine Chemicals Biosciences Collagen from rat tail Bornstein and Traub Type I | 9007-34-5 | MFCD00130825 | 10mg
Collagen from rat tail Bornstein and Traub Type IPurity: MW: | 9007-34-5 | MFCD00130825 | 10mg