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TXNL4B Protein, Human, Recombinant (His)

カタログ番号 TMPY-02723
別名: DLP, Dim2, thioredoxin-like 4B

Dim2, also known as TXNL4B, is a member of the DIM1 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. Despite 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. Dim2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids and having a molecular mass of 21.1kDa. It is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Dim2 has a vital role in pro-mRNA splicing. Dim2 is required in cell cycle progression for S/G2 transition and interacts with PRPF6 subunit of the spliceosome.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
TXNL4B Protein, Human, Recombinant (His)
パッケージサイズ 在庫状況 単価(税別)
100 μg 約5 days ¥ 161,000
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生物学的特性に関する説明
Technical Params
Product Properties
参考文献
説明 Dim2, also known as TXNL4B, is a member of the DIM1 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. Despite 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. Dim2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids and having a molecular mass of 21.1kDa. It is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Dim2 has a vital role in pro-mRNA splicing. Dim2 is required in cell cycle progression for S/G2 transition and interacts with PRPF6 subunit of the spliceosome.
Species Human
Expression Host E. coli
Tag His
Accession Number Q9NX01
別名 DLP, Dim2, thioredoxin-like 4B
Construction The Human TXNL4B (Q9NX01) (Met 1-Ile 149) was expressed, with a polyhistide tag at the N-terminus.
Protein Purity > 92 % as determined by SDS-PAGE
分子量 19 kDa (predicted)
Endotoxin Please contact us for more information.
Formulation Supplied as sterile PBS, 20% glycerol, 0.1% Tween20, 50 mM Arg, pH 7.5.
Reconstitution A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage

It is recommended to store the product under sterile conditions at -20℃ to -80℃. Samples are stable for up to 12 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

Shipping

In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.

Research Background Dim2, also known as TXNL4B, is a member of the DIM1 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. Despite 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. Dim2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids and having a molecular mass of 21.1kDa. It is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Dim2 has a vital role in pro-mRNA splicing. Dim2 is required in cell cycle progression for S/G2 transition and interacts with PRPF6 subunit of the spliceosome.

参考文献

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Keywords

TXNL4B Protein, Human, Recombinant (His) DLP Dim2 thioredoxin-like 4B recombinant recombinant-proteins proteins protein