Recombinant Human SNRPD2 protein is a Human Full Length protein, in the 1 to 118 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M S L L N K P K S E M T P E E L Q K R E E E E F N T G P L S V L T Q S V K N N T Q V L I N C R N N K K L L G R V K A F D R H C N M V L E N V K E M W T E V P K S G K G K K K S K P V N K D R Y I S K M F L R G D S V I V V L R N P L I A G K
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Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077).
SNRPD1, SNRPD2, Small nuclear ribonucleoprotein Sm D2, Sm-D2, snRNP core protein D2
Recombinant Human SNRPD2 protein is a Human Full Length protein, in the 1 to 118 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Purified using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077).
Belongs to the snRNP core protein family.
Previously labelled as SNRPD2.
This product was previously labelled as Sm-D2
The small nuclear ribonucleoprotein D2 (SNRPD2) also known as Sm-D2 is a component of the spliceosomal small nuclear ribonucleoproteins (snRNP) essential for pre-mRNA splicing. It has a molecular weight of approximately 14 kDa and is ubiquitously expressed in various tissues highlighting its significant function across different cell types. SNRPD2 is part of the Sm protein family which plays an important role in the assembly and function of spliceosomal snRNPs.
SNRPD2 participates in the formation of the spliceosomal core necessary for the removal of introns from pre-mRNA which is important for generating mature mRNA transcripts. This protein is a part of the spliceosome complex consisting of other snRNPs and numerous accessory proteins. SNRPD2's involvement in mRNA processing highlights its fundamental role in gene expression regulation affecting how cells translate genetic information into functional proteins.
SNRPD2 is a critical element in the spliceosome pathway a major route for the post-transcriptional modification of RNA. This pathway is integral to the regulation of alternative splicing events influencing protein diversity. SNRPD2 also interacts with other spliceosomal proteins such as SNRPB and SNRPE cooperating to facilitate precise exon-exon junctions. The fidelity of this pathway depends substantially on the integrity and functionality of SNRPD2 alongside its protein partners.
SNRPD2 shows a connection to autoimmune conditions such as systemic lupus erythematosus (SLE) where autoantibodies target snRNP components including SNRPD2. This autoimmune disorder may disrupt normal spliceosomal function contributing to disease pathology. Additionally alterations in splicing pathways involving SNRPD2 have links to certain cancers where dysregulated splicing can lead to oncogenic transformations. Understanding SNRPD2's role in these conditions may reveal therapeutic targets for modulating splicing in disease contexts.
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15% SDS-PAGE analysis of ab104481 (3 μg).
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