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AB121129

Anti-SNRPD3/Sm-D3 antibody

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(3 Publications)

Rabbit Polyclonal SNRPD3/Sm-D3 antibody. Suitable for WB, ICC/IF, IHC-P and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human SNRPD3 aa 1 to C-terminus.

View Alternative Names

Small nuclear ribonucleoprotein Sm D3, Sm-D3, snRNP core protein D3, SNRPD3

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SNRPD3/Sm-D3 antibody (AB121129)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SNRPD3/Sm-D3 antibody (AB121129)

ab121129 staining SNRPD3/Sm-D3 in Paraffin-emebedded Human small intestine tissue by Immunohistochemistry. Note : strong nuclear positivity in glandular cells.

Western blot - Anti-SNRPD3/Sm-D3 antibody (AB121129)
  • WB

Unknown

Western blot - Anti-SNRPD3/Sm-D3 antibody (AB121129)

All lanes:

Western blot - Anti-SNRPD3/Sm-D3 antibody (ab121129) at 1/250 dilution

Lane 1:

RT4 cell lysate

Lane 2:

U-251 MG cell lysate

Lane 3:

Human Plasma lysate

Lane 4:

Human Liver lysate

Lane 5:

Human Tonsil lysate

Predicted band size: 14 kDa

true

Immunocytochemistry/ Immunofluorescence - Anti-SNRPD3/Sm-D3 antibody (AB121129)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-SNRPD3/Sm-D3 antibody (AB121129)

Immunofluorescent staining of human cell line U-2 OS shows positivity in nucleus but excluded from the nucleoli.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, ICC/IF, WB

applications

Immunogen

Recombinant Fragment Protein within Human SNRPD3 aa 1 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

P62318

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

SNRPD3 also known as Sm-D3 is a protein that plays an important role in the assembly of small nuclear ribonucleoproteins (snRNPs) essential for pre-mRNA splicing. This protein has a molecular mass of approximately 10 kDa. It functions as a core component of the spliceosomal machinery an essential complex in eukaryotic gene expression. You can find SNRPD3 expressed in various tissues where pre-mRNA splicing activity is required reflecting its fundamental role in cellular processes.
Biological function summary

SNRPD3 participates in snRNP assembly by interacting with other Sm proteins to form a heptameric ring structure around small nuclear RNAs (snRNAs). As part of the major spliceosomal snRNPs SNRPD3 contributes to the modification and catalysis of pre-mRNA splicing. The protein also gets involved in RNA stability and regulation. As a member of the spliceosome complex SNRPD3 helps ensure the fidelity and precision of splicing events important for generating mature mRNA molecules.

Pathways

The actions of SNRPD3 lie within the splicing pathway and have implications in the gene expression pathway. Interaction occurs with other proteins such as SNRPD1 and SNRPD2 which are also part of the snRNP complex facilitating effective spliceosomal function. The U1 snRNP specifically involving SNRPD3 plays a part in the recognition of splice sites initiating the splicing of pre-mRNAs.

Issues with SNRPD3 function or expression might relate to autoimmune diseases such as lupus and some neurodegenerative conditions. Antinuclear antibodies targeting snRNP components including SNRPD3 are common in systemic lupus erythematosus indicating its involvement in the disease's pathology. Furthermore alterations in splicing mechanisms involving SNRPD3 might influence neurodegenerative disorders due to its role in RNA processing and stability potentially relating to other RNA-binding proteins like hnRNPs.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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 : 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, PubMed : 33509932). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing (By similarity).
See full target information SNRPD3

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Science advances 7: PubMed33762328

2021

Arginine methyltransferase PRMT5 negatively regulates cGAS-mediated antiviral immune response.

Applications

Unspecified application

Species

Unspecified reactive species

Dapeng Ma,Min Yang,Qiushi Wang,Caiyu Sun,Hongbiao Shi,Weiqiang Jing,Yuxuan Bi,Xuecheng Shen,Xiaomin Ma,Zhenzhi Qin,Yueke Lin,Lihui Zhu,Yunxue Zhao,Yeping Cheng,Lihui Han

Cell reports 30:1935-1950.e8 PubMed32049022

2020

Symmetric Arginine Dimethylation Is Selectively Required for mRNA Splicing and the Initiation of Type I and Type III Interferon Signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Patrick J Metz,Keith A Ching,Tao Xie,Paulina Delgado Cuenca,Sherry Niessen,John H Tatlock,Kristen Jensen-Pergakes,Brion W Murray

Life science alliance 1:e201800070 PubMed30456350

2018

Proteomics and neuropathology identify ribosomes as poly-GR/PR interactors driving toxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Hannelore Hartmann,Daniel Hornburg,Mareike Czuppa,Jakob Bader,Meike Michaelsen,Daniel Farny,Thomas Arzberger,Matthias Mann,Felix Meissner,Dieter Edbauer
View all publications

Product promise

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