LSM1 Homolog, U6 Small Nuclear RNA Associated (S. Cerevisiae) (LSM1) antibody

Details for Product No. ABIN141457
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Synonyms lsm1, NV45, CASM, YJL124C, 2810025O06Rik, zgc:101136
(55), (10), (8), (3), (2), (1), (1), (1), (1)
(29), (22), (3)
Western Blotting (WB)
(52), (17), (15), (15), (14), (8), (5), (2), (2), (1)
Pubmed 8 references available
Quantity 50 μg
Shipping to United States ( )
Immunogen Full length native protein (purified) (Human) LSM1.
Specificity Binds specifically to the 3-terminal U-tract of U6 snRNA LSm subunits form a heteromer with a donut shape.
Cross-Reactivity Mouse (Murine), Rat (Rattus)
Purification Immunogen affinity purified
Alternative Name LSM1 (LSM1 Antibody Abstract)
Background SM-like proteins were identified in a variety of organisms based on sequence homology with the SM protein family. SM-like proteins contain the SM sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The SM-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing.
Research Area Chromatin and Nuclear Signaling, DNA/RNA
Application Notes Recommended dilutions - WB: 1/2000. Predicted molecular weight: 15 kDa. We recommend using about 2.5 ug of positive control protein in the colorimetric method, and about 10x less for ECL detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
Restrictions For Research Use only
Concentration 1 mg/ml
Buffer PBS
Preservative Azide free
Storage -20 °C
Supplier Images
Image no. 1 for anti-LSM1 Homolog, U6 Small Nuclear RNA Associated (S. Cerevisiae) (LSM1) antibody (ABIN141457) anti-LSM1 Homolog, U6 Small Nuclear RNA Associated (S. Cerevisiae) (LSM1) antibody
Background publications Lehner, Sanderson: "A protein interaction framework for human mRNA degradation." in: Genome research, Vol. 14, Issue 7, pp. 1315-23, 2004 (PubMed).

Lehner, Semple, Brown et al.: "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region." in: Genomics, Vol. 83, Issue 1, pp. 153-67, 2003 (PubMed).

Ingelfinger, Arndt-Jovin, Lührmann et al.: "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci." in: RNA (New York, N.Y.), Vol. 8, Issue 12, pp. 1489-501, 2003 (PubMed).

Strausberg, Feingold, Grouse et al.: "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. ..." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 26, pp. 16899-903, 2002 (PubMed).

Takahashi, Suzuki, Inaguma et al.: "Down-regulation of Lsm1 is involved in human prostate cancer progression." in: British journal of cancer, Vol. 86, Issue 6, pp. 940-6, 2002 (PubMed).

Eystathioy, Peebles, Hamel et al.: "Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera." in: Arthritis and rheumatism, Vol. 46, Issue 3, pp. 726-34, 2002 (PubMed).

Salgado-Garrido, Bragado-Nilsson, Kandels-Lewis et al.: "Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin." in: The EMBO journal, Vol. 18, Issue 12, pp. 3451-62, 1999 (PubMed).

Schweinfest, Graber, Chapman et al.: "CaSm: an Sm-like protein that contributes to the transformed state in cancer cells." in: Cancer research, Vol. 57, Issue 14, pp. 2961-5, 1997 (PubMed).

Catalog No. ABIN141457
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