SMN1 Antibody (YA5063)
(Synonyms: SMN1; SMN; SMNT; SMN2; SMNC; Survival motor neuron protein; Component of gems 1; Gemin-1)SMN1 Antibody (YA5063) is a Rabbit-derived and non-conjugated monoclonal antibody, targeting to SMN1.
-
Host:
Rabbit
-
Isotype:
IgG
-
Application:
WB; IHC-P; IHC-F; IP; IF-Tissue
-
Reactivity :
Human, Mouse, Rat
-
Formulation:
Supplied in 10mM phosphate buffered saline(pH 7.4) with 150mM sodium chloride, 0.05% BSA, 0.02% Proclin300 and 50% glycerol.
-
Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
|
IHC-P
IHC-P: Immunohistochemistry-Paraffin
|
IHC-F
IHC-F: Immunohistochemistry-Frozen
|
IP
IP: Immunoprecipitation
|
IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
|
|---|---|---|---|---|---|
| Dilution Ratio | 1:500-2000 | 1:50-200 | 1:50-200 | 1:20-50 | 1:50-200 |
Product Details
SMN1 Antibody (YA5063) is a Rabbit-derived and non-conjugated monoclonal antibody, targeting to SMN1.
-
Host Rabbit
-
Clonality Monoclonal,Recombinant
-
Species ReactivityHuman, Mouse, Rat
-
Observed Molecular WeightObserved band size: 36 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
-
Calculated Molecular Weight Predicted band size: 32 kDa
A synthesized peptide derived from human SMN1. The exact sequence is proprietary to MCE.
Endogenous
affinity purified by Protein A
Non-conjugated
Unmodified
IgG
Product Properties
-
Appearance
Solution
-
Formulation
Supplied in 10mM phosphate buffered saline(pH 7.4) with 150mM sodium chloride, 0.05% BSA, 0.02% Proclin300 and 50% glycerol.
-
Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
-
Shipping
Shipping with blue ice.
Background
-
Function
SMN1 is a 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. 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). 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. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits. 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. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. 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. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)[1][2][3][4][5][6][7][8].
-
Subcellular Localization
Nucleus, gem; Nucleus, Cajal body; Cytoplasm; Cytoplasmic granule; Perikaryon; Cell projection, neuron projection; Cell projection, axon; Cytoplasm, myofibril, sarcomere, Z line
-
Expression
Tissue_specificity:It is expressed in a variety of tissues. High expression is observed in the brain, kidneys, and liver; moderate expression in skeletal muscle and cardiac muscle; and low expression in fibroblasts and lymphocytes. High expression is also observed in the spinal cord. Expression is also found in osteoclasts and monocytes (protein level) . -
Isoforms & Post-Translational Modification
SMN1 has 4 isomers: Q16637-1: 31849 Da (predicted); Q16637-2: 28534 Da (predicted); Q16637-3: 30450 Da (predicted); Q16637-4: 27135 Da (predicted).
-
Subunit
Homooligomer; may form higher order homooligomers in the dimer to octamer range Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Component of an import snRNP complex composed of KPNB1, RNUT1, SMN1 and ZNF259. Interacts with DDX20, FBL, NOLA1, RNUT1, SYNCRIP and with several spliceosomal snRNP core Sm proteins, including SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE and ILF3. Interacts with GEMIN2; the interaction is direct. Interacts with GEMIN3; the interaction is direct. Interacts with GEMIN8; the interaction is direct. Interacts with SNRPB; the interaction is direct.
-
SwissProt ID
-
Synonyms
SMN1; SMN; SMNT; SMN2; SMNC; Survival motor neuron protein; Component of gems 1; Gemin-1
Documentation
References
[1]. Chari A, et al. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell. 2008 Oct 31;135(3):497-509. [Content Brief]
[2]. Pellizzoni L, et al. A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing. Cell. 1998 Nov 25;95(5):615-24. [Content Brief]
[3]. Otter S, et al. A comprehensive interaction map of the human survival of motor neuron (SMN) complex. J Biol Chem. 2007 Feb 23;282(8):5825-33. [Content Brief]
[4]. Zhang R, et al. Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly. Cell. 2011 Aug 5;146(3):384-95. [Content Brief]
[5]. Tripsianes K, et al. Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nat Struct Mol Biol. 2011 Nov 20;18(12):1414-20. [Content Brief]
[6]. Yi H, et al. Negative cooperativity between Gemin2 and RNA provides insights into RNA selection and the SMN complex's release in snRNP assembly. Nucleic Acids Res. 2020 Jan 24;48(2):895-911. [Content Brief]
[7]. Lotti F, et al. An SMN-dependent U12 splicing event essential for motor circuit function. Cell. 2012 Oct 12;151(2):440-54. [Content Brief]
[8]. Zhao DY, et al. SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination. Nature. 2016 Jan 7;529(7584):48-53. [Content Brief]
Powered by Bioz
