Adipogen/anti-Survival Motor Neuron Protein (human), mAb (7B10)/AG-20T-0003-C200/200 µg一抗
SMN; Gemin-1; Component of Gems 1; BCD541
Recombinant human full-length survival motor neuron protein (SMN).
Used for purification of native tagged proteins and RNA-protein complexes.
Optimal conditions must be determined individually for each application.
Recognizes a sequence of up to 9 amino acids in the N-terminal domain of human SMN.
Protein A/G purified.
Liquid. In PBS and 0.02% sodium azide.
Shipping and Handling
Short Term Storage
Long Term Storage
Avoid freeze/thaw cycles.
Stable for at least 1 year after receipt when stored at -20°C.
Product Specification Sheet
The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. It may also play a role in the metabolism of snoRNPs. It is expressed in a wide variety of tissues, including high levels in brain, kidney and liver, moderate levels in skeletal and cardiac muscle and low levels in fibroblasts and lymphocytes. Mutations in SMN cause spinal muscular atrophy 1 (SMA1). Spinal muscular atrophy is a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, le
ng to symmetrical muscle weakness and atrophy. The antibody was used extensively to purify and characterize the macromolecular SMN complex from cultured human cells. The antibody binds with high affinity and specificity to its epitope, which comprises a sequence of up to 9 amino acids in the N-terminal part of human SMN. It allows the native elution of bound antigen with an excess of the cognate peptide. Via addition of the 7B10 epitope (TagIt epitope) to other proteins this purification strategy can also be exploited for purification of these fusion proteins and RNA-protein complexes from cells lacking this epitope on endogenous proteins, such as cells derived from
Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins: G. Meister, et al.; Hum. Mol. Gen.
A multiprotein complex mediates the ATPdependent assembly of spliceosomal U snRNPs: G. Meister, et al.; Nature Cell
Direct interaction of the spinal muscular atrophy disease protein SMN with the small nucleolar RNA-associated protein fibrillarin: K.W: Jones, et al.; J. Biol. Chem.
Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs: G. Meister & U. Fischer; EMBO J.
Coilin methylation regulates nuclear body formation: M.D. Hebert, et al.; Dev. Cell
SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin β: U. Narayanan, et al.; Hum. Mol. Gen.
Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein: U. Narayanan, et al.; Mol. Cell
Phosphorylation regulates the activity of the SMN complex during assembly of spliceosomal U snRNPs: M. Grimmler, et al.; EMBO Rep.
Unrip, a factor implicated in cap-independent translation, associates with the cytosolic SMN complex and influences its intracellular localization: M. Grimmler, et al.; Hum. Mol. Genet.
A Comprehensive Interaction Map of the Human Survival of Motor Neuron (SMN) Complex: S. Otter, et al.; J. Biol. Chem.
Evolution of an RNP assembly system: a minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster: M. Kroiss, et al.; PNAS
Native purification of protein and RNA-protein complexes using a novel affinity procedure: M. Kroiss, et al.; Fly