Rabbit Recombinant Monoclonal SMN/Gemin 1 antibody - conjugated to Alexa Fluor® 647.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:18984161, PubMed:9845364). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161). Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits (PubMed:17178713, PubMed:21816274, PubMed:22101937). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625). Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development (PubMed:23063131). Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).
SMN, SMNT, SMN2, SMNC, SMN1, Survival motor neuron protein, Component of gems 1, Gemin-1
Rabbit Recombinant Monoclonal SMN/Gemin 1 antibody - conjugated to Alexa Fluor® 647.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 68% PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
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This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
Alexa Fluor® is a registered trademark of Molecular Probes, Inc, a Thermo Fisher Scientific Company. The Alexa Fluor® dye included in this product is provided under an intellectual property license from Life Technologies Corporation. As this product contains the Alexa Fluor® dye, the purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). As this product contains the Alexa Fluor® dye the sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: in manufacturing; (ii) to provide a service, information, or data in return for payment (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are sold for use in research. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.
SMN also known as Survival of Motor Neuron protein or Gemin 1 is an important protein involved in the assembly of small nuclear ribonucleoproteins (snRNPs). It has a molecular mass of approximately 38 kDa. SMN proteins are expressed in almost all tissues with highest levels in spinal cord and brain tissues. They play a mechanical role in Gemin complex assisting RNA processing tasks which are essential in RNA metabolism alongside other Gemin proteins.
The SMN protein operates within the SMN-Gemin complex a multi-protein assembly important for snRNP biogenesis and pre-mRNA splicing. This complex coordinates the maturation and transport of snRNPs facilitating the processing of precursor mRNAs in the nucleus. SMN and associated Gemin proteins mediate the assembly of Sm proteins onto snRNA ensuring accurate splicing mechanisms necessary for gene expression.
The SMN protein is notably involved in the chaperone-assisted assembly pathway related to snRNP biogenesis. It plays a central role in the spliceosome assembly process working closely with Sm proteins and other RNA-binding proteins. Importantly SMN interacts with the ribonucleoprotein complex influencing mRNA splicing which integrates into the broader cell signaling pathways such as the cholinergic agonist pathways and RNA splicing pathways that regulate neuromuscular communication.
The deficiency or malfunction of SMN protein directly relates to Spinal Muscular Atrophy (SMA) an autosomal recessive disorder. SMA is characterized by motor neuron degeneration which can be attributed to insufficient SMN protein levels leading to compromised snRNP assembly and splicing. The SMN1 gene deletion or mutation reduces the available SMN protein linking this defect with the severity of SMA. Studies suggest that altering the expression levels of the related SMN2 gene can potentially modulate disease outcomes further emphasizing the connection between SMN protein and SMA pathogenesis.
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