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DIM1 / TXNL4A Antibody, Rabbit PAb

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    Human TXNL4A Antibody Product Information
    Immunogen:Recombinant Human DIM1 / TXNL4A protein (Catalog#12434-H07E)
    Clone ID:
    Ig Type:Rabbit IgG
    Concentration:
    Endotoxin:
    Formulation:0.2 μm filtered solution in PBS with 5% trehalose
    Preparation:Produced in rabbits immunized with purified, recombinant Human DIM1 / TXNL4A (rh DIM1 / TXNL4A; Catalog#12434-H07E; P83876; Met1-Tyr142). Total IgG was purified by Protein A affinity chromatography.
    Other TXNL4A Antibody Products
    DIM1/TXNL4A Background

    DIM1, also known as TXNL4A, is a member of the Dim protein family. The Dim protein family is composed of two classes, DIM1and Dim2, which share a common thioredoxin-like fold. They were originally identified for their role in cell cycle progression and have been found to interact with Prp6, an essential component of the spliceosome, which forms the bridge of U4/U6.U5-tri-snRNP. In spite of their biological and structural similarities, DIM1 and Dim2 proteins differ in many aspects. DIM1 bears distinctive structural motifs responsible for its interaction with other spliceosome components. Dim2 forms homodimers and contains specific domains required for its interactions with partners. This originality suggests that although both proteins are involved in pre-mRNA splicing, they are likely to be involved in different biological pathways. DIM1 interacts with HNRPF, HNRPH2, NEDD9/HEF1 and PQBP1/NPW38. It plays an essential role in pre-mRNA splicing.

    Human DIM1/TXNL4A References
  • Zhang Y, et al. (2001) Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Gene. 257 (1): 33-43.
  • Zhang YZ, et al. (2003) Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis. Biochemistry. 42(32):9609-18.
  • Zhang Y, et al. (2000) Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Gene. 257 (1):33-43.
  • Zhang YZ, et al. (2000) The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily. Physiol Genomics. 1(3):109-18.
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    Catalog: 12434-RP01-100
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    Datasheet & Documentation

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    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"