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

Details for Product No. ABIN141457
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Antigen
Synonyms lsm1, NV45, CASM, YJL124C, 2810025O06Rik, zgc:101136
Reactivity
Human
(33), (9), (6), (2), (1), (1), (1), (1)
Host
Chicken
(18), (13), (1)
Clonality
Polyclonal
Application
Western Blotting (WB)
(32), (11), (11), (10), (7), (4), (2), (1), (1)
Pubmed 8 references available
Quantity 50 μg
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Catalog No. ABIN141457
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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
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
anti-LSM1 Homolog, U6 Small Nuclear RNA Associated (S. Cerevisiae) (LSM1) antibody anti-LSM1 Homolog, U6 Small Nuclear RNA Associated (S. Cerevisiae) (LSM1) antibody
General 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).

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).

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).

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).

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).

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).

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).

Lehner, Sanderson: "A protein interaction framework for human mRNA degradation." in: Genome research, Vol. 14, Issue 7, pp. 1315-23, 2004 (PubMed).

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