|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Glutaminyl-tRNA Synthetase (QARS) antibody
|Synonyms||GLNRS, PRO2195, Aast-g1n, BcDNA:GH11673, GlnRS, QRS, l(3)05461, qars, Dmel\CG10506, CG10506, C80286, MGC105238, 1110018N24Rik, 1200016L19Rik, Qars, MGC94241, MGC56395, zgc:56395, QARS, EPRS, MGC128695|
Alternatives ELISA, Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
|5 references available|
|Quantity||0.1mg (0.5 mg/ml)|
|Price||450.00 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Immunogen||QARS (NP_005042, 677 a.a. ~ 776 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 K|
|Description||Other names: GLNRS, PRO2195glutaminyl-tRNA synthetase|
|Characteristics||Purified Mouse Monoclonal Antibody (Mab)|
|Specificity||QARS (NP_005042, 677 a.a. ~ 776 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.|
|Molecular Weight||87799 DA|
Background: Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.
|Application Notes||ELISA ~~ 1ug/ml~3ng/ml Western blot ~~ 1:500~1000 Immunohistochemistry ~~ 1.5ug/ml|
|Buffer||Clear, colorless solution in phosphate buffered saline, pH 7.2 .|
|Storage||Maintain refrigerated at 2-8 deg C for up to 6 months. For long term storage store at -20 deg C in small aliquots to prevent freeze-thaw cycles|
|Research Area||Cell Structure|
|Restrictions||For Research Use only|
Gerhard, Wagner, Feingold et al.: "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." in: Genome research, Vol. 14, Issue 10B, pp. 2121-7, 2004 (PubMed).
Rush, Moritz, Lee et al.: "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." in: Nature biotechnology, Vol. 23, Issue 1, pp. 94-101, 2005 (PubMed).
Ling, Yao, Zheng et al.: "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex." in: The Journal of biological chemistry, Vol. 280, Issue 41, pp. 34755-63, 2005 (PubMed).
Stelzl, Worm, Lalowski et al.: "A human protein-protein interaction network: a resource for annotating the proteome." in: Cell, Vol. 122, Issue 6, pp. 957-68, 2005 (PubMed).
Rual, Venkatesan, Hao et al.: "Towards a proteome-scale map of the human protein-protein interaction network." in: Nature, Vol. 437, Issue 7062, pp. 1173-8, 2005 (PubMed).
|Hosts||Rabbit (10), Mouse (1)|
|Reactivities||Human (10), Mouse (Murine) (3), Rat (Rattus) (3)|
|Applications||Western Blotting (WB) (10), Immunohistochemistry (IHC) (6), ELISA (5), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)) (1), Immunoprecipitation (IP) (1)|
|Epitopes||N-Term (3), C-Term (1)|