Recombinant Human TXNL4B Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4706

Recombinant Human TXNL4B Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4706
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Product Overview

Tag His
Host Species Human
Accession Q9NX01
Synonym Dim2, DLP
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. 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. Dim2 roduced 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.
Description A DNA sequence encoding the human TXNL4B (Q9NX01) (Met 1-Ile 149) was expressed, with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met 1-Ile 149
Molecular Weight The recombinant human TXNL4B consisting of 165 a.a. and migrates as an approximately 19 KDa band in SDS-PAGE under reducing conditions as predicted.
Purity >92% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 20% glycerol, 0.1% Tween20, 50mM Arg, pH 7.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Essential role in pre-mRNA splicing. Required in cell cycle progression for S/G(2) transition.
Subcellular Location Nucleus.
Protein Families DIM1 family
Database References

Gene Functions References

  1. A crystal structure of TXNL4B was determined at 1.33 A resolution and refined to an Rwork of 0.13 and an Rfree of 0.18 with one native dimer in the asymmetric unit. PMID: 23519793
  2. DLP is implicated in not only cell cycle progression but also in a more specific molecular process such as pre-mRNA splicing PMID: 15161931
  3. crystal structure; in contrast to hDim1, hDim2 forms stable homodimers PMID: 16142897
  4. The human gene coding for the spliceosomal protein thioredoxin-like 4B (TXNL4B) was overexpressed in Escherichia coli and the encoded protein was purified and crystallized. PMID: 16511018

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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