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AB150383

Anti-Gemin 2 antibody [EPR10040(B)]

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(2 Publications)

Rabbit Recombinant Monoclonal Gemin 2 antibody. Suitable for WB and reacts with Human, Mouse, Rat samples. Cited in 2 publications.

View Alternative Names

SIP1, GEMIN2, Gem-associated protein 2, Gemin-2, Component of gems 2, Survival of motor neuron protein-interacting protein 1, SMN-interacting protein 1

1 Images
Western blot - Anti-Gemin 2 antibody [EPR10040(B)] (AB150383)
  • WB

Unknown

Western blot - Anti-Gemin 2 antibody [EPR10040(B)] (AB150383)

All lanes:

Western blot - Anti-Gemin 2 antibody [EPR10040(B)] (ab150383) at 1/1000 dilution

Lane 1:

HepG2 cell lysate at 10 µg

Lane 2:

K562 cell lysate at 10 µg

Lane 3:

HeLa cell lysate at 10 µg

Secondary

All lanes:

HRP labeled goat anti-rabbit at 1/2000 dilution

Predicted band size: 31 kDa

false

  • Carrier free

    Anti-Gemin 2 antibody [EPR10040(B)] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR10040(B)

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA
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.

Gemin 2 also known simply as "gemin" is a protein identified by its mass of approximately 29 kDa. The protein is an essential component in the survival of motor neuron (SMN) complex. Gemin 2 localizes mainly in the cytoplasm and is expressed in a variety of tissues throughout the body with a notable presence in motor neurons. This protein works closely within a multi-protein assembly regulating several functions related to the synthesis and processing of RNA.
Biological function summary

Gemin 2 plays a role in the assembly of small nuclear ribonucleoproteins (snRNPs) which are integral to pre-mRNA splicing. As part of the SMN complex Gemin 2 ensures the proper assembly and delivery of snRNPs to the spliceosome. This activity is necessary for accurate splicing of pre-mRNA which is a critical step in gene expression. The protein's binding and interaction capabilities stabilize this complex contributing to efficient splicing processes.

Pathways

Gemin 2 is integral to RNA processing mechanisms and the RNP biogenesis pathway. It associates with other proteins like Gemin 6 and Gemin 7 within the SMN complex to promote snRNP biogenesis and function. Additionally Gemin 2 contributes to pathways that oversee proper mRNA processing and stability ensuring that gene expression is accurately regulated in the cell.

Mutations or dysfunctions in the Gemin 2 protein are linked with spinal muscular atrophy (SMA) a neurodegenerative disorder affecting motor neurons. In SMA the SMN complex including Gemin 2 is disrupted leading to deficits in snRNP assembly and widespread splicing defects. Also disruptions in this protein may have connections to muscular dystrophies where imbalances in splicing can cause muscle weakness and atrophy. Gemin 2's interplay with the SMN protein is particularly significant in these disorders as their interaction is critical for maintaining motor neuron function and viability.

Product protocols

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

Target data

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 : 9323129). 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 (5Sm) 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 (PubMed : 18984161, PubMed : 9323129). 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). Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound (PubMed : 16314521, PubMed : 21816274, PubMed : 31799625).
See full target information GEMIN2

Publications (2)

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

Cell reports. Medicine 5:101659 PubMed39067446

2024

Isogenic patient-derived organoids reveal early neurodevelopmental defects in spinal muscular atrophy initiation.

Applications

Unspecified application

Species

Unspecified reactive species

Tobias Grass,Zeynep Dokuzluoglu,Felix Buchner,Ines Rosignol,Joshua Thomas,Antonio Caldarelli,Anna Dalinskaya,Jutta Becker,Fabian Rost,Michele Marass,Brunhilde Wirth,Marc Beyer,Lorenzo Bonaguro,Natalia Rodriguez-Muela

The Journal of clinical investigation 128:3008-3023 PubMed29672276

2018

Blocking p62-dependent SMN degradation ameliorates spinal muscular atrophy disease phenotypes.

Applications

Unspecified application

Species

Unspecified reactive species

Natalia Rodriguez-Muela,Andrey Parkhitko,Tobias Grass,Rebecca M Gibbs,Erika M Norabuena,Norbert Perrimon,Rajat Singh,Lee L Rubin
View all publications

Product promise

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