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MOUSE ANTI HUMAN CD261

ArtNr 20-783-315076
Hersteller GENWAY
Menge 25 ug
Kategorie
Typ Antibody
Applikationen IP
Specific against Human (Homo sapiens)
Host Mouse
ECLASS 10.1 32160702
ECLASS 11.0 32160702
UNSPSC 12352203
Alias GWB-A3E37D
Similar products 20-783-315076
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Genway ID:
GWB-A3E37D
Specificity:
CD261
Isotype:
IgG1
Preparation:
Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
Buffer Solution:
Phosphate buffered saline pH7. 4
Preservative Stabilisers:
0. 09% Sodium AzideApprox. Protein Concentrations: IgG concentration 1. 0 mg/ml
Immunogen:
Fusion protein containing the extracellular region of CD261 (DR4).
Specificity:
Is specific for human death receptor 4 (DR4) also known as CD261 or TRAIL- R1. DR4 is a type I transmembrane protein of 468 amino acids which is expressed in most human tissues including spleen peripheral blood leucocytes thymus and in a variety of tumour-derived cell lines. DR4 plays a role in inducing cell death. The binding of TRAIL to DR4 triggers the activation of pro-caspases 8 and 10 leading to apoptosis. Recommended Negative Controls: MOUSE IgG1 NEGATIVE CONTROLRecommended Secondary Antibodies: Rabbit Anti Mouse IgGGoat Anti Mouse IgGGoat Anti Mouse IgG (H/L)Goat Anti Mouse IgG IgA IgMHuCAL Anti Mouse IgG1Goat Anti Mouse IgG (Fc)Sheep Anti Mouse IgG (H/L)
Function:
Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Ref. 7Subunit structureCan interact with TRADD and RIP. Interacts with ARAP1. Ref. 9Subcellular locationMembrane; Single-pass type I membrane protein. Tissue specificityWidely expressed. High levels are found in spleen peripheral blood leukocytes small intestine and thymus but also in K562 erythroleukemia cells MCF7 breast carcinoma cells and activated T-cells. Sequence similaritiesContains 1 death domain. Contains 3 TNFR-Cys repeats. 1. Krauhs E. et al. (1981) Complete amino acid sequence of beta-tubulin from porcine brain. P. N. A. S. 78: 4156-4160. 2. Draber P. et al. (1990) Inhibition of microtubule assembly in vitro by anti-tubulin monoclonal antibodies. FEBS Lett. 262: 209-211. [1] \" Complete amino acid sequence of beta-tubulin from porcine brain. \" Krauhs E. Little M. Kempf T. Hofer-Warbinek R. Ade W. Ponstingl H. Proc. Natl. Acad. Sci. U. S. A. 78:4156-4160(1981) [PubMed: 6945576] [Abstract]Cited for: PROTEIN SEQUENCE. Tissue: Brain. [2] \" The GTP-binding peptide of beta-tubulin. Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins. \" Linse K. Mandelkow E. M. J. Biol. Chem. 263:15205-15210(1988) [PubMed: 3170578] [Abstract]Cited for: PROTEIN SEQUENCE OF 63-77. [3] \" Localization of the ATP binding site on alpha-tubulin. \" Zabrecky J. R. Cole R. D. Arch. Biochem. Biophys. 225:475-481(1983) [PubMed: 6688710] [Abstract]Cited for: GUANINE NUCLEOTIDE-BINDING SITES. [4] \" The 4 A X-ray structure of a tubulin:stathmin-like domain complex. \" Gigant B. Curmi P. A. Martin-Barbey C. Charbaut E. Lachkar S. Lebeau L. Siavoshian S. Sobel A. Knossow M. Cell 102:809-816(2000) [PubMed: 11030624] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3. 95 ANGSTROMS). [5] \" Structure of the alpha beta tubulin dimer by electron crystallography. \" Nogales E. Wolf S. G. Downing K. H. Nature 391:199-203(1998) [PubMed: 9428769] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3. 7 ANGSTROMS) OF 1-427. [6] \" 15 A resolution model of the monomeric kinesin motor KIF1A. \" Kikkawa M. Okada Y. Hirokawa N. Cell 100:241-252(2000) [PubMed: 10660047] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (15. 0 ANGSTROMS). [7] \" Refined structure of alpha beta-tubulin at 3. 5 A resolution. \" Loewe J. Li H. Downing K. H. Nogales E. J. Mol. Biol. 313:1045-1057(2001) [PubMed: 11700061] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3. 5 ANGSTROMS).

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