Recombinant Human PDHA1 Protein (aa 30-390, His & GST Tag)

Name: Recombinant Human PDHA1 Protein (aa 30-390, His & GST Tag)
Brand: Beta LifeScience
SKU: BLPSN-3735
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His&GST
Host Species	Human
Accession	P08559
Synonym	PDHA, PDHAD, PDHCE1A, PHE1A
Background	PDHA1, also known as C54G1, is an alpha subunit of pyruvate dehydrogenase. Pyruvate dehydrogenase, together with dihydrolipoamide acetyltransferase and lipoamide dehydrogenase, composes the pyruvate dehydrogenase (PDH) complex. The PDH complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. PDHA1 plays a key role in the function of the PDH complex. Defects in PDHA1 can cause pyruvate dehydrogenase E1-alpha deficiency. Defects in PDHA1 also are the cause of X-linked Leigh syndrome (X-LS). X-LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord.
Description	A DNA sequence encoding the human PDHA1 (P08559-1) (Phe30-Ser390) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Phe30-Ser390
Molecular Weight	The recombinant human PDHA1/GST chimera consists of 598 a.a. and has a calculated molecular mass of 68 kDa. The recombinant protein migrates as an approximately 65 kDa band in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 20mM Tris, 500mM Nacl, 3mM DTT, 10% gly, pH 8.0..
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	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular Location	Mitochondrion matrix.
Database References	HGNC: 8806 OMIM: 300502 KEGG: hsa:5160 UniGene: Hs.530331
Associated Diseases	Pyruvate dehydrogenase E1-alpha deficiency (PDHAD)
Tissue Specificity	Ubiquitous.

Gene Functions References

Case demonstrates fetal akinesia deformation sequence due to a de novo hemizygous c.498C > T splice-site mutation in the pyruvate dehydrogenase-alpha 1 (PDHA1) gene. PMID: 28495245
Data show that metformin reduces hypoxia-inducible factor 1alpha (HIF-1alpha) gene expression and increases pyruvate dehydrogenase (PDH) expression. PMID: 27474170
The report PDHA1 as a new component of brainstem-type Lewy bodies in idiopathic PD, DLB and PARK14, the level of PDHA1 protein being significantly decreased in the putamen and substantia nigra of patients with idiopathic Parkinson's disease . PMID: 28564592
Findings show that serine-threonine-tyrosine kinase 1 (NOK) mediates glycolysis and nuclear pyruvate dehydrogenase complex (PDC) associated histone acetylation. PMID: 28410146
The association of mitochondrial microphthalmia-associated transcription factor (MITF) with pyruvate dehydrogenase (PDH) emerges as an important regulator of mast cell function. Our findings indicate that PDH could arise as a new target for the manipulation of allergic diseases. PMID: 27871875
our results show that negative PDHA1 gene expressionis associated with significantly higher cell stemness in prostate cancer cells and reduced protein expression of this gene is associated with shorter clinical outcome in prostate cancers. PMID: 28076853
oncoprotein HBXIP enhances glucose metabolism reprogramming through suppressing SCO2 and PDHA1 in breast cancer PMID: 26309161
Lack of PDHE1alpha protein expression is associated with Esophageal Squamous Cell Carcinoma. PMID: 26408721
MPO and BPI in CD4(+)T-lymphocytes, and PDHA1 and MRPL42 in CD8(+) T-lymphocytes might be used as specific biomarkers of severe asthma progression. PMID: 26107902
Phosphorylation at distinct serine and tyrosine residues inhibits PDHA1 through distinct mechanisms to impact active site accessibility. PMID: 25104357
High HK2 expression combined with low phosphorylated PDHA1 expression in the invasive front lesions of colorectal tumors is predictive of tumor aggressiveness and survival. PMID: 25060325
In the presence of PPARbeta/delta, Vpr induced a 3.3-fold increase in PPAR response element-driven transcriptional activity, a 1.9-fold increase in PDK4 protein expression, and a 1.6-fold increase in the phosphorylated pyruvate dehydrogenase subunit E1alpha. PMID: 23842279
In this study the phenotypes of patients with PDH deficiency have been divided into three groups of mutations. PMID: 19517265
Expression of the PDHA1 gene was found in all somatic cells, whereas expression of PDHA2 gene was restricted to germ cells. The switch from X-linked to autosomic gene expression occurred in spermatocytes. PMID: 22750801
Molecular analysis of PDH1A revealed a novel hemizygous c.1045G>A mutation, predicting a p.A349T missense mutation. PMID: 22142326
Skin fibroblast culture assay revealed PDH deficiency, confirmed by mutation analysis of the E1 alpha subunit. PMID: 21895644
TNFalpha can inhibit pulmonary artery smooth muscle cells pyruvate dehydrogenase activity and induce a pulmonary arterial hypertension phenotype. PMID: 21809123
We provide an efficient stepwise strategy for mutation screening in pyruvate dehydrogenase complex genes and expand the growing list of PDHA1 mutations analyzed at the structural level PMID: 21914562
Data show that overexpression of ErbB2 maintains PDH flux by suppressing PDK4 expression in an Erk-dependent manner. PMID: 21852536
4 affected female patients with PDHA1 mutations who had with severe cortical atrophy, dilated ventricles, and an incomplete corpus callosum. PMID: 21723463
We document the broad variability of clinical symptoms of pdha1 deficiency disease. We proved that normal PDHc activity may not exclude the disease. PMID: 21470495
Novel nonsense mutation (R263X) of the E1alpha subunit in pyruvate dehydrogenase complex deficiency PMID: 20958858
PDHA1 mutations were screened in 40 patients with biochemically demonstrated pyruvate dehydrogenase complex deficiency deficiency or strong clinical suspicion and changes with probable pathological significance were found in 20. PMID: 20002461
AAV3-mediated transfer and expression of the pyruvate dehydrogenase E1 alpha subunit gene causes metabolic remodeling and apoptosis of human liver cancer cells. PMID: 19586787
model of the pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and binding of the E1 and E3 components PMID: 14638692
determinant spreading might underlie the autoimmunity against Elalpha. PMID: 14708897
PDHA1 gene mutations may have a role in Pyruvate dehydrogenase E1 subunit deficiency PMID: 16713755
Molecular genetic analysis of the X-chromosomal E1alpha subunit of PDH showed three new mutations in phylogenetically conserved areas of the protein: Glu358Lys in patient 1; Arg88Lys in patient 2 and 3 (brothers); and Leu216Ser in patient 4. PMID: 16967364
Short-term elevation in plasma non-esterified fatty acids at rest increases PDH-E1alpha phosphorylation, but exercise overrules this effect and phosphorylation leads to even dephosphorylation during exercise with intralipid infusion. PMID: 17065338
Attenuated PDHa activity contributes to the preferential oxidation of n-6 PUFA during moderate-intensity exercise. PMID: 17947500
Resting PDH protein content and phosphorylation on PDH-E1 alpha sites 1 and 2 were higher in vastus lateralis than in triceps and deltoid as was the activity of oxidative enzymes PMID: 17957032
two synonymous mutations expand the spectrum of rare PDHA1 splicing mutations, all of which are located in non canonical splice sites. PMID: 18023225
Our results encourage the use of amino acid supplementation to overcome the metabolic/biochemical changes induced by PDHA1 gene specific mutations associated with mild pyruvate dehydrogenase complex phenotypes. PMID: 18398624

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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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