Recombinant Human PTMA Protein (GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3958

Recombinant Human PTMA Protein (GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3958
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Product Overview

Tag GST
Host Species Human
Accession P06454
Synonym TMSA
Background PTMA (prothymosin, alpha, N-GST chimera) is a small, 12.4 kDa protein. It is a 19-111 amino acid long polypeptide as the precursor of thymosin a1. Thymosins are named becaues they were originally isolated from the thymus. But now in many other tissues, thymosins also can be detected. Thymosins have diverse biological activities, and two in particular, thymosins a1 and _4, have potentially important uses in medicine, some of which have already progressed from the laboratory to the clinic. In general, PTMA is associated with cellular proliferation and carcinogenesis (Eschenfeldt et al., 1986), cellular and viral transcription (Cotter et al., 2), protection against apoptosis and chromatin remodelling (Karetsou et al., 1998). PTMA may have a dual role both intracellulary and extracellulary. In relation to diseases, thymosins have been categorized as biological response modifiers. Thymosin a1 is derived from PTMA. For animals that lack thymus glands, thymosin a1 is responsible for the activity of that preparation in restoring immune function.
Description A DNA sequence encoding the human PTMA (P06454-1) (Ser 2-Asp 111) was fused with the GST tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Ser 2-Asp 111
Molecular Weight The recombinant human PTMA/GST chimera consists of 341 a.a. and has a predicted molecular mass of 39 kDa. It migrates as an approxiamtely 45 KDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 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 Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
Subcellular Location Nucleus.
Protein Families Pro/parathymosin family
Database References

Gene Functions References

  1. According to the cellular function of the characterized targets of ProTalpha, and the evolution in the composition of the diverse ProTalpha-complexes when proliferation activity was reduced or apoptosis induced, leads to hypothesized that ProTalpha interactions might be related to the proliferation activity and control of the cell survival. PMID: 29106904
  2. Prothymosin-alpha variants elicit anti-HIV-1 response via TLR4 dependent and independent pathways. PMID: 27310139
  3. PTMA is a potential novel therapeutic target for type 2 diabetes PMID: 26348351
  4. disease-free survival and overall survival rates were significantly lower among colorectal cancer patients with PTMA- and TP53-positive tumors PMID: 25197357
  5. Data suggest that KEAP1 (kelch-like ECH-associated protein 1) mutations (as those observed in lung cancer patients) affect conformation/folding/stability of KEAP1 and binding affinity for ligands PTMA and NRF2 (nuclear factor erythroid 2-like 2). PMID: 25582950
  6. Data suggest that plasma thymosin-alpha1 (TA1) and prothymosin-alpha (PTMA) level may be a biomarker for differentiating between renal cell carcinoma (RCC) and urothelial carcinoma. PMID: 22609059
  7. prothymosin-alpha expression is a determinant of disease progression in superficial bladder cancer PMID: 24733561
  8. PTalpha offers cardioprotection against ischemic injury by an Akt-dependent mechanism. PMID: 23857453
  9. phosphorylation of ProTalpha is required for its antiapoptotic activity, but it does not affect its nuclear import PMID: 23859021
  10. These results demonstrate the clinical relevance of prothymosin alpha in regulating acetylation events during the pathogenesis of emphysema. PMID: 23695700
  11. Western blot analysis of protein extracts from sperm head fractions confirms that the peptide is specifically associated with the inner acrosomal membrane fraction. PMID: 23359453
  12. ProTalpha is crucial for the interaction with the Kelch domain, while the flanking residues play relatively minor roles in the affinity of binding. PMID: 23318954
  13. The decrease of ProTalpha mRNA during differentiation was not accompanied by changes in the methylation status PMID: 22463375
  14. The prothymosin alpha is one of miR-1 target genes which involve in miR-1 inducing apoptosis PMID: 22059741
  15. Findings suggest that the binding of prothymosin alpha (ProTalpha) and Neh2 to Keap1 occurs synergistically via preformed structural elements. PMID: 22125611
  16. The PTMA is one of miR-1 target genes which involve in miR-1 inducing apoptosis. PMID: 22059741
  17. when added to cultured cells expressing mHtt, the purified recombinant ProTalpha protein not only entered the cells but it also significantly suppressed the mHtt-caused cytotoxicity. PMID: 22110140
  18. Nuclear PTMA may serve as prognostic marker in head and neck squamous cell carcinoma to determine the subset of patients that are likely to show recurrence of the disease. PMID: 21573209
  19. These results are consistent with the model that ProTa may enhance p53 transcription activity by displacement of histone H1 from p53-H1 repressive complex. PMID: 21954601
  20. A study on the relationship between prothymosin alpha kinase(ProTalphaK) activity and pyruvate kinase isoforms confirmed that the M2 isoform is the enzyme responsible for ProTalphaK activity in proliferating cells. PMID: 20977946
  21. Data suggest that prothymosin alpha immunostaining may be helpful in predicting pituitary tumor recurrence. PMID: 20430720
  22. Prothymosin alpha amino acid residues 4-14, 31-43, 84-87, and 106-110 strongly and specifically bind to apoptotic protease activating factor 1 (Apaf-1) in the regulation of the mitochondrial cell death pathway. PMID: 20121050
  23. we demonstrate the existence of three binding partners (31, 29, and 19 kDa) for ProTalpha in the membrane of PHA-activated lymphoblasts. These surface molecules possess the expected affinity and specificity for a ProTalpha receptor PMID: 11727831
  24. prothymosin alpha is capable of forming regular elongated fibrils PMID: 12062405
  25. regulatory roles of oncoprotein ProT and tumor suppressor PHAP in apoptosis PMID: 12522243
  26. study suggests involvement of prothymosin a, in the formation, maintenance, or functioning of the mitotic spindle PMID: 15325071
  27. PTMA associates with SET and is involved in chromatin decondensation. PMID: 15556635
  28. Prothymosin alpha functions as intranuclear dissociator of the Nrf2-Keap1 complex. PMID: 15657435
  29. PTMA expression is intimately involved in the differentiation and progression of human prostate cancers, and could be a target for therapy and diagnostic purposes. PMID: 16353248
  30. Antiapoptotic response of cells requires expression of both p8 and ProTalpha. PMID: 16478804
  31. the anti-apoptotic effect previously attributed separately to p8 and prothymosin alpha is in fact borne by the p8/ProTalpha complex, the two proteins being individually inactive PMID: 16628001
  32. Marked differences in the expression of PTMA and Tim10 were observed during the differentiation of human primary skeletal muscle cells. PMID: 16669873
  33. suppression of viral replication by ProTalpha is not HIV LTR specific PMID: 16940531
  34. interaction of ProTalpha with core histones in the nucleus may be related to structural modification of histones H3 & H4, & hence to chromatin activity, raising the possibility that other proteins in the nuclear complex may play a role in this process. PMID: 17012289
  35. Decreased ERbeta and increased ProTalpha expression in advanced gastric adenocarcinoma indicated that ERbeta may play an anti-proliferation role which is opposed to the role of ProTalpha in gastric epithelium. PMID: 17046193
  36. although prothymosin-alpha is overexpressed in gastric adenocarcinoma, it is not associated with alterations in survival PMID: 17188166
  37. PTMA may be a novel marker for predicting the effectiveness of radiotherapy in clinical cases. PMID: 17876542
  38. Basis on site-specific information obtained here, as well as results from previous studies, we propose that the conformational and dynamic changes upon zinc binding may act as an entropic switch that greatly facilitates the binding to other proteins PMID: 17929838
  39. ProTalpha and Nrf2 compete for interaction with Keap1, therefore ProTalpha is able to liberate Nrf2 from complex with Keap1 and hence contribute to Nrf2-dependent transcription. PMID: 18240569
  40. Influence of prothymosin alpha and its mutants on activity of the p53 tumor suppressor PMID: 18856068
  41. immune response stimulation by ProTalpha is in principle exerted via its bioactive C-terminal decapaptide, which can acquire a sequence-specific beta-sheet conformation and induce DC maturation. PMID: 18976813
  42. induces unravelling of metaphase chromosomes in vitro PMID: 11528108

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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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