Recombinant Human Camp-Dependent Protein Kinase Catalytic Subunit Alpha (PRKACA) Protein (His)

Name: Recombinant Human Camp-Dependent Protein Kinase Catalytic Subunit Alpha (PRKACA) Protein (His)
Brand: Beta LifeScience
SKU: BLC-11071P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Camp-Dependent Protein Kinase Catalytic Subunit Alpha (PRKACA) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P17612
Target Symbol	PRKACA
Synonyms	cAMP dependent protein kinase alpha catalytic subunit; cAMP dependent protein kinase beta catalytic subunit; cAMP dependent protein kinase catalytic beta subunit isoform 4ab; cAMP dependent protein kinase catalytic subunit alpha; cAMP dependent protein kinase catalytic subunit alpha, isoform 1; cAMP dependent protein kinase catalytic subunit beta; cAMP-dependent protein kinase catalytic subunit alpha; KAPCA_HUMAN; PKA C alpha ; PKA C beta; PKA C-alpha; PKACA; PKACB; PPNAD4; PRKACA; PRKACAA; PRKACB ; Protein kinase A catalytic subunit alpha; Protein kinase A catalytic subunit; Protein kinase A catalytic subunit beta; Protein kinase, cAMP dependent, catalytic, alpha; Protein kinase, cAMP dependent, catalytic, beta
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Expression Range	2-351aa
Protein Length	Full Length of Mature Protein
Mol. Weight	44.5
Research Area	Cancer
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.
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	Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in chondrogenesis by mediating phosphorylation of SOX9. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock.; Phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.
Subcellular Location	Cytoplasm. Cell membrane. Nucleus. Mitochondrion. Membrane; Lipid-anchor.; [Isoform 2]: Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome.
Protein Families	Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
Database References	HGNC: 9380 OMIM: 601639 KEGG: hsa:5566 STRING: 9606.ENSP00000309591 UniGene: PMID: 29259079 CaV1.4 channels are indeed modulated by PKA phosphorylation within the inhibitor of Ca(2+)-dependent inactivation (ICDI) motif. PMID: 27456671 In this study, the authors linked for the first time the loss of RIIbeta protein levels to the PRKACA mutation status and found the down-regulation of RIIbeta to arise post-transcriptionally. PMID: 28250426 the presence of lipofuscin in cortisol-producing adenomas (CPAs) responsible for Cushing syndrome with and without the PRKACA (pLeu206Arg) somatic mutation, was investigated. PMID: 28834963 Mechanistically, Sirt1 expression elevates phosphorylation of the alpha subunit of protein kinase A (PKA alpha), and this event is essential for Sirt1-induced phosphorylation of beta Catenin. PMID: 28583374 PKA, under the conditions of experimental approach appears to function as a master upstream kinase that is sufficient to initiate the complex pattern of intracellular signaling pathway and gene expression profiles that accompany ovarian granulosa cells differentiation PMID: 27324437 CTR activates AKAP2-anchored cAMP-dependent protein kinase A, which then phosphorylates tight junction proteins ZO-1 and claudin 3. PMID: 28428082 These results indicate that Mixed fibrolamellar hepatocellular carcinoma (mFL-HCC) is similar to pure FL-HCC at the genomic level and the DNAJB1:PRKACA fusion can be used as a diagnostic tool for both pure and mFL-HCC PMID: 27029710 PRKACA mutations are highly specific for cortisol over-secretion, while they are absent or very rare in the context of other adrenal diseases. Patients carrying these somatic mutations are affected by a more severe phenotype and are identified at a younger age. PMID: 27871112 Somatic mutations in PRKACA, coding for the catalytic alpha subunit of protein kinase A (PKA), have been recently identified as the most frequent genetic alteration in cortisol-secreting adrenocortical adenomas, which are responsible for adrenal Cushing's syndrome. PMID: 27813054 HIF1a transcriptional activity is stimulated by Protein kinase A-dependent phosphorylation PMID: 27245613 cigarette smoke extracts activate the PKA, CREB, and IL-13Ralpha2 axis in lung endothelial cells. PMID: 27986643 Data indicate a subpopulation of the CaV1.2 channel pore-forming subunit (alpha1C) within nanometer proximity of protein kinase A (PKA) at the sarcolemma of murine and human arterial myocytes. PMID: 28119464 we propose that the PKA-Smurf1-PIPKIgamma pathway has an important role in pulmonary tumorigenesis and imposes substantial clinical impact on development of novel diagnostic markers and therapeutic targets for lung cancer treatment. PMID: 28581524 cAMP/PKA signaling attenuated respiratory syncytial virus-induced disruption of structure and functions of the model airway epithelial barrier by mechanisms involving the stabilization of epithelial junctions and inhibition of viral biogenesis PMID: 28759570 The mutated PRKACA proteins lost their ability to bind to PRKAR1A, and thereby lead to constitutive activation of the PKA pathway. Together with previous reports of PRKAR1A mutations in syndromic cardiac myxoma, our study demonstrates the importance of the PKA pathway in the tumourigenesis of cardiac myxoma. PMID: 28369983 differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II. PMID: 27160899 Data show that the adenylate cyclase (AC) pathway as genes relating to the antitumor activity of xanthohumol (XN) against tumor cells, and the pathway regulates various cellular functions via activating protein kinase A (PKA)-dependent phosphorylation. PMID: 28122154 PRKACA mutations are present in cortisol-producing adenomas and bilateral adrenal macronodular hyperplasia. PRKACA mutation is associated with more severe autonomous cortisol secretion. PMID: 27296931 Dual co-expression of human fetal Tau with PKA in Escherichia coli results in multisite Tau phosphorylation including also naturally occurring sites which were not previously considered in the context of 14-3-3 binding. Tau protein co-expressed with PKA displays tight functional interaction with 14-3-3 isoforms of a different type. PMID: 28575131 This review will discuss the effects of PKA phosphorylation on wild-type CFTR, the consequences of cystic fibrosis mutations on PKA phosphorylation, and the development of therapies that target PKA-mediated signaling. [review] PMID: 27722768 This interaction is promoted by EPAC1 activation, triggering its translocation to the plasma membrane and binding to NHERF1. Our findings identify a new CFTR-interacting protein and demonstrate that cAMP activates CFTR through two different but complementary pathways - the well-known PKA-dependent channel gating pathway and a new mechanism regulating endocytosis that involves EPAC1. PMID: 27206858 The inhibitory effects of BMP4 on PDGF-induced cell proliferation, collagen synthesis, and calpain-2 activation are impaired in pulmonary artery smooth muscle cells from pulmonary arterial hypertension patient. PMID: 28235949 immunohistochemical staining for StAR is a reliable pathological approach for the diagnosis and classification of adrenocortical adenomas with cAMP/PKA signaling-activating mutations. PMID: 27606678 description of PRKACA mutations in 2 cases of primary aldosteronism (PA) patients: a novel variant (p.His88Asp) in a case of sudden onset of PA and a mutation (p.Leu206Arg) in context of hypokalemic aggravation of long-term hypertension; these genetic alterations were not found in a subsequent series of 120 aldosterone-producing adenomas and thereby appear to be very rare events PMID: 27270477 PKA signaling is pivotal in pigmentation process itself in cultured melanoma cells, while the importance of Wnt/beta-catenin signaling should be emphasized in the context of development and differentiation PMID: 27567978 Studies indicate a functional interaction between leucine-rich repeat kinase 2 (LRRK2) and protein kinase A (PKA) cross-talk in neuron and microglia. PMID: 28202680 Studies indicate the 3'-5'-Cyclic adenosine monophosphate/protein kinase A (cAMP/PKA) signalling pathway at distinct mitochondria subdomains represented by the outer and inner mitochondrial membranes. PMID: 28202681 CKbeta phosphorylation by MCF-7 cell lysate was inhibited by a PKA-specific inhibitor peptide, and the intracellular phosphorylation of CKbeta was shown to be regulated by the level of cyclic adenosine monophosphate (cAMP), a PKA activator PMID: 27149373 GPER enhances melanogenesis via PKA by upregulating microphthalmia-related transcription factor-tyrosinase in melanoma PMID: 27378491 testosterone rapidly increased whole-cell HCAEC SKCa and BKCa currents via a surface androgen receptor, Gi/o protein, and protein kinase A PMID: 28223151 PRKACA mutation is associated with Adrenocortical Adenomas. PMID: 27389594 Differentiation of mesenchymal stem cells into beige/brown adipocytes can be related via PKA modulation. PMID: 27498007 FL-HCCs in children and young adults uniquely overexpress DNAJB1-PRKACA, which results in elevated cAMP-dependent PKA activity PMID: 27027723 high-resolution models for PKA(WT) and PKA(L)(205R) substrate specificity. PMID: 28100013 CFTR inhibition also affected cAMP/PKA-downstream events such as the increase in tyrosine phosphorylation, hyperactivated motility, and acrosome reaction. PMID: 27714810 Results suggest that G protein alpha S subunit (Galphas) plays a tumor-promoting role in renal cell carcinoma (RCC) and possibly acts through a protein kinase A (PKA)-dependent pathway. PMID: 28051330 Phosphorylation of ezrin together with its binding to phosphatidylinositol-4,5-bisphosphate tethers the F508del CFTR to the actin cytoskeleton, stabilizing it on the apical membrane and rescuing the sub-membrane compartmentalization of cAMP and activated PKA. PMID: 26823603 Data show that activated PKA phosphorylates the 19S subunit, Rpn6/PSMD11 (regulatory particle non-ATPase 6/proteasome subunit D11) at Ser14. PMID: 26669444 Our results reveal for the first time the role of the versatile PKA in cancer cells survival under chronic glucose starvation and anoikis and may be a novel potential target for cancer treatment. PMID: 26978032 PKA phosphorylates the ATPase inhibitory factor 1 and inactivates its capacity to bind and inhibit the mitochondrial H(+)-ATP synthase. PMID: 26387949 DNAJB1-PRKACA was evaluated as a key driver of fibrolamellar carcinoma and as a candidate therapeutic target PMID: 26505878 No somatic mutations were observed in PRKACA in a cohort of GH-secreting pituitary adenomas. PMID: 26701869 Protein kinase A activity is necessary for fission and fusion of Golgi to endoplasmic reticulum retrograde tubules. PMID: 26258546 Kapbeta2 interacts with ULK2 through ULK2's putative PY-NLS motif, and facilitates transport from the cytoplasm to the nucleus, depending on its Ser1027 residue phosphorylation by PKA, thereby reducing autophagic activity. PMID: 26052940 ITM2A expression is positively regulated by PKA-CREB signaling and ITM2A expression interferes with autophagic flux by interacting with vacuolar ATPase. PMID: 25951193 Akt and PKA phosphorylated KLHL3 at S433, and phosphorylation of KLHL3 by PKA inhibited WNK4 degradation. PMID: 26435498 Data indicate that protein kinase A (PKA) phosphorylates only serine-253 amino acid on activator of G-protein signaling 1 protein Dexras1 (RASD1). PMID: 26358293 PKA compartmentalization via AKAP220 and AKAP12 contributes to endothelial barrier regulation. PMID: 25188285 Leu206Arg and Leu199_Cys200insTrp mutations in PRKACA impair its association with PRKAR2B and PRKAR1A. PMID: 25477193

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.