Recombinant Human Pyruvate Dehydrogenase E1 Component Subunit Alpha, Somatic Form, Mitochondrial (PDHA1) Protein (GST)

Name: Recombinant Human Pyruvate Dehydrogenase E1 Component Subunit Alpha, Somatic Form, Mitochondrial (PDHA1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-06250P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Pyruvate Dehydrogenase E1 Component Subunit Alpha, Somatic Form, Mitochondrial (PDHA1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P08559
Target Symbol	PDHA1
Synonyms	PDHE1-A type I
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	ANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS
Expression Range	31-390aa
Protein Length	Partial
Mol. Weight	67.6 kDa
Research Area	Metabolism
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	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: 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.

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