Recombinant Human Prothymosin Alpha (PTMA) Protein (His)

Name: Recombinant Human Prothymosin Alpha (PTMA) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03478P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Prothymosin Alpha (PTMA) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P06454
Target Symbol	PTMA
Synonyms	Prothymosin alpha (gene sequence 28); Prothymosin alpha; Prothymosin alpha like 1 protein; PTMA; PTMA_HUMAN; Thymalfasin; Thymosin alpha 1 acetate; Thymosin alpha 1; Thymosin alpha; Thymosin alpha-1; TMSA
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-10His
Target Protein Sequence	MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAENEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD
Expression Range	1-111aa
Protein Length	Full Length
Mol. Weight	14.7kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 9623 OMIM: 188390 KEGG: hsa:5757 STRING: 9606.ENSP00000344547 UniGene: Hs.459927

Gene Functions References

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
Prothymosin-alpha variants elicit anti-HIV-1 response via TLR4 dependent and independent pathways. PMID: 27310139
PTMA is a potential novel therapeutic target for type 2 diabetes PMID: 26348351
disease-free survival and overall survival rates were significantly lower among colorectal cancer patients with PTMA- and TP53-positive tumors PMID: 25197357
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
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
prothymosin-alpha expression is a determinant of disease progression in superficial bladder cancer PMID: 24733561
PTalpha offers cardioprotection against ischemic injury by an Akt-dependent mechanism. PMID: 23857453
phosphorylation of ProTalpha is required for its antiapoptotic activity, but it does not affect its nuclear import PMID: 23859021
These results demonstrate the clinical relevance of prothymosin alpha in regulating acetylation events during the pathogenesis of emphysema. PMID: 23695700
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
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
The decrease of ProTalpha mRNA during differentiation was not accompanied by changes in the methylation status PMID: 22463375
The prothymosin alpha is one of miR-1 target genes which involve in miR-1 inducing apoptosis PMID: 22059741
Findings suggest that the binding of prothymosin alpha (ProTalpha) and Neh2 to Keap1 occurs synergistically via preformed structural elements. PMID: 22125611
The PTMA is one of miR-1 target genes which involve in miR-1 inducing apoptosis. PMID: 22059741
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
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
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
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
Data suggest that prothymosin alpha immunostaining may be helpful in predicting pituitary tumor recurrence. PMID: 20430720
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
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
prothymosin alpha is capable of forming regular elongated fibrils PMID: 12062405
regulatory roles of oncoprotein ProT and tumor suppressor PHAP in apoptosis PMID: 12522243
study suggests involvement of prothymosin a, in the formation, maintenance, or functioning of the mitotic spindle PMID: 15325071
PTMA associates with SET and is involved in chromatin decondensation. PMID: 15556635
Prothymosin alpha functions as intranuclear dissociator of the Nrf2-Keap1 complex. PMID: 15657435
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
Antiapoptotic response of cells requires expression of both p8 and ProTalpha. PMID: 16478804
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
Marked differences in the expression of PTMA and Tim10 were observed during the differentiation of human primary skeletal muscle cells. PMID: 16669873
suppression of viral replication by ProTalpha is not HIV LTR specific PMID: 16940531
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
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
although prothymosin-alpha is overexpressed in gastric adenocarcinoma, it is not associated with alterations in survival PMID: 17188166
PTMA may be a novel marker for predicting the effectiveness of radiotherapy in clinical cases. PMID: 17876542
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
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
Influence of prothymosin alpha and its mutants on activity of the p53 tumor suppressor PMID: 18856068
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
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.

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