Recombinant Mouse Protein kinase C alpha type(Prkca)

Code CSB-YP018699MO
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Source Yeast
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Code CSB-EP018699MO
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Source E.coli
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Code CSB-EP018699MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP018699MO
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Source Baculovirus
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Code CSB-MP018699MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Prkca
Uniprot No. P20444
Alternative Names Prkca; PkcaProtein kinase C alpha type; PKC-A; PKC-alpha; EC 2.7.11.13
Species Mus musculus (Mouse)
Expression Region 2-672
Target Protein Sequence ADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS LLYGLIHQGM KCDTCDMNVH KQCVINDPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSNLN PQWNESFTFK LKPSDKDRRL SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKAHNQ EEGEYYNVPI PEGDEEGNME LRQKFEKAKL GPVGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLNNVM LNSEGHIKIA DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKQPAKR LGCGPEGERD VREHAFFRRI DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN PQFVHPILQS AV
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Data

Function Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP. Depending on the cell type, is involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation. In cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Depending on the cell type, exhibits anti-apoptotic function and protects cells from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, or mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (By similarity). Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.
Gene References into Functions
  1. Deleting the Prkca gene, which encodes PKCalpha, reverses diabetes-induced autophagy impairment, cellular organelle stress and apoptosis, leading to an NTD reduction. PKCalpha increases the expression of miR-129-2, which is a negative regulator of autophagy. miR-129-2 represses autophagy by directly targeting PGC-1alpha, a positive regulator for mitochondrial function, which is disturbed by maternal diabetes. PMID: 28474670
  2. Its pathway may promote reactive oxygen species generation in the early state Alzheimer's disease and eventually contribute to the exacerbation of pathological phenotype PMID: 29602494
  3. This indicates a role for PKC in dynamically controlling the trafficking of SNAT3 transporters in astrocytes in situ. PMID: 29561757
  4. Results show that de novo polarisation of the embryo at the 8-cell stage is directed by phospholipase C (PLC) and protein kinase C (PKC). PMID: 29030553
  5. protein kinase Calpha (PKCalpha) gain of function mutations may promote synaptic defects in Alzheimer's disease PMID: 27165780
  6. PKC-alpha plays a crucial role in the pathophysiology of peritoneal membrane dysfunction induced by peritoneal dialysis fluids, and its therapeutic inhibition might be a valuable treatment option for peritoneal dialysis patients. PMID: 27142955
  7. these results identify PKCalpha and HMGB1 as important co-regulators involved in hydrogen peroxide-induced poly-ADP-ribose formation. PMID: 27198223
  8. We conclude that synaptotagmin-1 phosphorylation is an essential step in PKC-dependent potentiation of synaptic transmission, acting downstream of the two other essential DAG/PKC substrates, Munc13-1 and Munc18-1. PMID: 27091977
  9. Kinocilium is essential for proper localization of Lgn, as well as Gai and aPKC, suggesting that cilium function plays a role in positioning of apical proteins critical for hearing. PMID: 26662512
  10. Social defeat-driven PKA activation in the basolateral amygdala is actually a compensatory rather than pathogenic response in the homeostasis. PMID: 26747511
  11. PKCalpha deficiency leads to pulmonary vascular hyperresponsiveness to TXA2, possibly via increased pulmonary arterial TP receptor expression. PMID: 26890419
  12. PKC gene deletion is responsible for hair loss. PMID: 26076315
  13. The overall result suggests the cancer preventive activity of quercetin via the induction of apoptosis and modulates PKC signaling with the reduction of oxidative stress in ascite cells of lymphoma-bearing mice. PMID: 26076811
  14. the ANG II-dependent upregulation of renin in the collecting duct depends on PKC-alpha, which allows the augmentation of cAMP production and activation of PKA/CREB pathway PMID: 26268270
  15. role for PKCalpha in the regulation of ECM structure and deposition during skin wound healing. PMID: 26354149
  16. A dynamic PKC phosphorylation/de-phosphorylation cycle of Munc18-1 drives short-term enhancement of transmitter release during post-tetanic potentiation. PMID: 24520164
  17. PKC-alpha and -delta have been shown to play crucial role in cardiac adaptation during physiological and pathological hypertrophy respectively thereby rendering compromised cardiac function to an otherwise efficient heart by conditional reversal of activation. PMID: 25116170
  18. Data show increased expression of T-type Ca(2+) current and association of protein kinase C alpha (PKCalpha) with caveolin-3 (Cav-3)was disrupted in the hypertrophic ventricular myocyte. PMID: 26170457
  19. These results suggest that mechanisms of PKC-induced hypersensitivity of TRPV1 are modality specific and that S800 is a polymodal sensitization site integrating multiple inflammatory signals in nociceptors. PMID: 25734989
  20. Protein kinase C phosphorylation of a Pcdhgc3c-terminal lipid binding domain regulates FAK inhibition and dendrite arborization. PMID: 26139604
  21. Protein kinase C alpha plays an important modulatory role in RBCs, regulating both the peak amplitude and temporal properties of the RBC light response in the rod visual pathway. PMID: 26230760
  22. These results demonstrate the importance of PKCbetaII in chronic lymphocytic leukemia-like disease progression and suggest a role for PKCalpha subversion in creating permissive conditions for leukemogenesis. PMID: 25616575
  23. The results of this study findings indicate that PKCdelta plays a role in mediating histamine-induced itch, but may be dispensable for chloroquine- and beta-alanine-induced itch PMID: 25558916
  24. Study demonstrates that PKCalpha, PKCdelta and PKCepsilon isoforms are differentially expressed in particular cellular components of pre-pubertal, pubertal and adult mouse ovarian follicles. PMID: 25491605
  25. regulates UT-A1 function by increasing glycan sialylation through Src kinase pathways PMID: 25300290
  26. PKC-alpha activation and interaction with F0F1-ATPase improves F0F1-ATPase activity and ATP content in injured renal cells. PMID: 25627689
  27. PKCalpha expression is associated with a delayed replacement of embryonic smooth muscle by skeletal muscle at the distal esophagus and consecutive megaesophagus PMID: 24862691
  28. These results suggest that mitochondrial APE1/Ref-1 is contributed to the protective role to protein kinase C-induced mitochondrial dysfunction in endothelial cells. PMID: 24861944
  29. PKC-alpha and -betaIotaIota are the predominant isoforms in the developing optic pathway, whereas PKC-epsilon is the major form in the chiasmatic neurons. PMID: 24863469
  30. Genetic ablation of PKCalpha preserves AQP2 and UT-A1 protein expression and localization in lithium-induced nephrogenic diabetes insipidus. PMID: 25006961
  31. contributes to high NaCl-dependent activation of NFAT5 through ERK1/2 PMID: 25391900
  32. These findings implicate PKCalpha as a target gene for therapeutic approaches in low bone mass conditions. PMID: 25070889
  33. In summary, our results indicate that cytoskeleton perturbation via PKCalpha and PKCdelta inactivation potentiates vascular calcification through osteogenic signal induction. PMID: 25445591
  34. Overexpressed PKCdelta downregulates the expression of PKCalpha in B16F10 melanoma. PMID: 24632809
  35. Stimulation by either PAF or ATP resulted in PKCalpha-mediated phosphorylation of LPCAT2 to enhance lyso-PAFAT activity and rapid PAF production. PMID: 24742674
  36. Polycystin-1 binds Par3/PKCalpha and controls convergent extension during renal tubular morphogenesis. PMID: 24153433
  37. Elevation of protein kinase Calpha stimulates osteogenic differentiation of mesenchymal stem cells. PMID: 24219286
  38. Identified a set of 22 alternative splicing events that undergo a developmental switch in splicing, and we confirmed that splicing reverts to an embryonic pattern in adult diabetic hearts. PKC isozymes alpha/beta control alternative splicing of these genes. PMID: 24151077
  39. Evaluated the effects of small interference RNA protein kinase C-alpha (siRNA-PKCalpha) on experimental proliferative vitreoretinopathy (PVR) induced by dispase in mice. PMID: 23626468
  40. Sirolimus-FKBP12.6 impairs endothelial barrier function by activation of protein kinase C-alpha and downstream disruption of the p120-VE cadherin interaction in vascular endothelium. PMID: 23887639
  41. Our findings indicate that PKCalpha and theta; contribute to T-cell activation with overlapping functions essential for graft-vs-host disease PMID: 23908466
  42. PAB induced cell cycle arrest, autophagy and senescence in murine fibrosarcoma L929 cell through Protein kinase C. PMID: 23630435
  43. PKCalpha and PKCbeta cooperate in IL-2 transcriptional transactivation in primary mouse T cells independently of the actions of PKCtheta;. PMID: 23439007
  44. PGE2-induced activation of angiogenesis is mediated via syndecan-4-dependent activation of PKCalpha. PMID: 23525101
  45. These results support the hypothesis that PKC-alpha and PKC-beta contribute to the pathogenesis of diabetic nephropathy, and that dual inhibition of the classical PKC isoforms is a suitable strategy for the prevention and treatment of diabetic nephropathy. PMID: 23434935
  46. This study aimed to investigate the functional and molecular changes of detrusor smooth muscle (DSM) in high-fat insulin resistant obese mice, focusing on the role of protein kinase C (PKC) and Ca(v)1.2 in causing bladder dysfunction. PMID: 23144896
  47. PKCalpha and Akt modulate platelet function by phosphorylating and inhibiting GSK3alpha/beta, thereby relieving the negative effect of GSK3alpha/beta on thrombin-mediated platelet activation. PMID: 23239877
  48. The elucidated signaling cascade explains how 5-HT(1A)-R regulates hippocampal sculpting and function, which may determine the affective phenotype of an adult. PMID: 22832728
  49. It was concluded that PKCalpha mediates hypertonicity-stimulated urea transport but is not necessary for vasopressin stimulation of urea permeability in mouse inner medullary collecting ducts. PMID: 23097465
  50. Follicle-stimulating hormone-induced activation of PKC alpha alone, or together with the inactivation of PKC betaI in granulosa cells, participates in mouse oocyte meiotic resumption. PMID: 23028752

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Involvement in disease Expression of the mutant form UV25 causes malignant transformation of cells.
Subcellular Location Cytoplasm, Cell membrane, Peripheral membrane protein, Mitochondrion membrane, Peripheral membrane protein, Nucleus
Protein Families Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
Database Links

KEGG: mmu:18750

STRING: 10090.ENSMUSP00000062392

UniGene: Mm.222178

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