Recombinant Human 14-3-3 / YWHAQ Protein

Beta LifeScience SKU/CAT #: BLPSN-0008

Recombinant Human 14-3-3 / YWHAQ Protein

Beta LifeScience SKU/CAT #: BLPSN-0008
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Product Overview

Host Species Human
Accession P27348
Synonym 1C5, 41701, HS1
Background The recently identified 14-3-3 tau, whose corresponding gene name is YWHAQ, is in a hypoxia-treated human trophoblast cell line. YWHAQ may play a role in epigenetic regulation of placental genes in the onset of Preeclampsia (PE). Moreover, there was a closer relationship between blood pressure and methylation levels of the YWHAQ promoter.
Description A DNA sequence encoding the human YWHAQ (P27348) (Met 1-Asn 245) was fused with the GST tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met 1-Asn 245
Molecular Weight The recombinant human YWHAQ/GST chimera consists of 476 a.a. and has a predicted molecular mass of 54.6 kDa. It migrates as an approxiamtely 53 kDa band in SDS-PAGE under reducing conditions.
Purity >88% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM Tris, 0.15m NaCl, 20mM GSH, pH 7.5.
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 Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.
Subcellular Location Cytoplasm. Note=In neurons, axonally transported to the nerve terminals.
Protein Families 14-3-3 family
Database References
Tissue Specificity Abundantly expressed in brain, heart and pancreas, and at lower levels in kidney and placenta. Up-regulated in the lumbar spinal cord from patients with sporadic amyotrophic lateral sclerosis (ALS) compared with controls, with highest levels of expression

Gene Functions References

  1. Chk1 and 14-3-3 proteins cooperate to inactivate the transcriptional repressor functions of atypical E2F proteins. This mechanism might be of particular importance to cancer cells, since they are exposed frequently to DNA-damaging therapeutic reagents. PMID: 29363506
  2. results suggest that PKC SUMOylation is an important regulator of the 14-3-3 and GluK2a protein complex and may contribute to regulate the decay kinetics of kainate receptor-excitatory postsynaptic currents PMID: 28837400
  3. Results show that 14-3-3zeta promotes cell proliferation, migration and invasion in lung adenocarcinoma. 14-3-3zeta upregulates MUC1 expression through enhancing MUC1/NFkappaB feedback loop. Its high expression is associated with poor survival in lung adenocarcinoma patients. PMID: 28901525
  4. TGFbetaR1 signaling was involved in 14-3-3zeta-mediated cell proliferation and metastasis of lung squamous cell carcinoma cells. PMID: 27764818
  5. Loss of Par3 promotes metastatic behavior in lung adenocarcinoma cells through 14-3-3zeta protein. PMID: 27588399
  6. this study reveals that 14-3-3zeta plays a critical role in Wnt5a/ROR1 signaling, leading to enhanced CLL migration and proliferation. PMID: 28465528
  7. Our results indicate that TRIM25 is associated with cisplatin resistance and 14-3-3sigma-MDM2-p53 signaling pathway is involved in this process, suggesting targeting TRIM25 may be a potential strategy for the reversal of cisplatin resistance. PMID: 28867193
  8. Up-regulation of 14-3-3zeta in response to pVHL is important for the recruitment of PI3K to the cell membrane and for stabilization of soluble beta-catenin. PMID: 28666999
  9. The 14-3-3 family is dysregulated in schizophrenia, perhaps owing to specific regulatory mechanisms; the expression of the 14-3-3 epsilon, theta and zeta isoforms could be useful indicators of disease severity. PMID: 27030512
  10. High urine 14-3-3 expression is associated with Advanced Stage in Patients with Clear Cell Renal Cell Carcinoma. PMID: 27039779
  11. Levels of 14-3-3 protein predict poorer radiographic outcomes in inflammatory polyarthritis patients. PMID: 26832367
  12. Study shows that 14-3-3 zeta/delta is important in the extracellular vesicles mediated induction of colon malignant phenotype, suggesting its role as a potential target for therapeutic interventions. PMID: 26231887
  13. the effects of cell viability, migration and invasion were mediated in 14-3-3zeta-dependent manner while that of cell apoptosis was mediated in 14-3-3zeta-independent manner. PMID: 26054824
  14. 14-3-3zeta reduces DNA damage by interacting with and stabilizing proliferating cell nuclear antigen PMID: 25169136
  15. phosphorylation of HS1 tyrosines at positions 222, 378 and 397 was required for transendothelial migration of NK cells. PMID: 25723543
  16. Mimitin and 14-3-3 protein zeta/delta are potential markers of paclitaxel resistance and prognostic factors in ovarian cancer. PMID: 26033570
  17. 14-3-3S is an interesting protein biomarker with the potential to further improve the accuracy of differential diagnostic process of hepatocellular tumors. PMID: 25448011
  18. The observed participation of 14-3-3 tau in the regulation of the placental epigenome may participate in the molecular mechanisms that govern the pathological process of preeclampsia, although this requires further evaluation. PMID: 25305692
  19. Epigenetic silencing of 14-3-3sigma occurred more frequently in the chronic inflammation group than in cancer patients and healthy controls. PMID: 25041782
  20. 14-3-3epsilon is involved in the regulation of cell cycle control, apoptosis, adhesion, carbohydrate metabolism, and nucleic acid metabolism. PMID: 24363202
  21. CCL20 and 14-3-3 zeta are molecules that play a putative role during tumorgenesis in pancreas, and may therefore be new parameters for histological diagnosis and discrimination between pancreatic neoplasms and chronic pancreatitis. PMID: 24629487
  22. Significant down-regulation of brain 14-3-3 levels were identified during prion infection. PMID: 24135906
  23. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin. [review] PMID: 24564655
  24. Using gene reporter assays, we show that promoter variations in 11 intrinsic apoptosis genes, including ADPRT, APAF1, BCL2, BAD, BID, MCL1, BIRC4, BCL2L1, ENDOG, YWHAB, and YWHAQ, influence promoter activity in an allele-specific manner. PMID: 24038028
  25. 14-3-3s not only can bind and regulate the activity of multiple phosphoproteins, but also possess moonlighting chaperone-like activity PMID: 24681339
  26. Data indicate that 14-3-3 zeta, gamma, epsilon, and tau isoforms but not the sigma protein hydrolyze ATP. PMID: 24269678
  27. Non-sigma 14-3-3 proteins synergized with ETV1 to activate transcription. PMID: 23774214
  28. 14-3-3 negatively regulates the RGC downstream of the PI3-kinase/Akt signaling pathway PMID: 23386617
  29. Data demonstrated that 14-3-3tau enhances the transcriptional activity of PR-B. PMID: 22967481
  30. this mini-review attempts to collect and to describe the data concerning monomers of 14-3-3.[review] PMID: 23159940
  31. a weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode PMID: 22952583
  32. An isoform-specific role for 14-3-3 protein is associated with atherosclerotic lesions of the cerebral and carotid arteries. PMID: 22405925
  33. Cerebrospinal fluid protein 14-3-3 detection remains an important test in the diagnosis of Creutzfeldt-Jakob disease. PMID: 23012332
  34. egradation of antiapoptosis protein 143-3beta induced by PrP106-126 peptide may be one of pathogenesis mechanism of prion disease PMID: 22978167
  35. LRFN4 complexed with 14-3-3s and NCK1 to mediate elongation in monocytic cells via Rac-1-mediated actin cytoskeleton reorganization PMID: 22677168
  36. 14-3-3 interacts with nonphosphorylated tau and promotes its interaction with and phosphorylation by a number of protein kinases. PMID: 21876254
  37. It was shown that ARF6 competes with 14-3-3 for binding to centralspindlin such that midbodies formed by centralspindlin mutants that can bind 14-3-3 but not ARF6 frequently collapse before abscission. PMID: 22580824
  38. autophosphorylation of Thr336 acts as an activating signal for LKB1 to recruit 14-3-3, which in turn attenuates the activation of LKB1 to keep the activity of LKB1 in check. PMID: 22575644
  39. 14-3-3 theta/tau and tBID have roles as predictive biomarkers of neoadjuvant chemotherapy resistance in breast cancer PMID: 22115752
  40. Altered 14-3-3 expression in brain can contribute to synaptic dysfunction and altered neurotransmission in chronic alcohol misuse by human subjects. PMID: 21332526
  41. Results suggest that the 14-3-3 protein binding affects the structure of the Galpha interaction portion of RGS3 as well as sterically blocks the interaction between the RGS domain and the Galpha subunit of heterotrimeric G proteins. PMID: 22027839
  42. 14-3-3 proteins mediate CaR-dependent Rho signalling and may modulate the plasma membrane expression of the CaR. PMID: 22010828
  43. 14-3-3beta has oncogenic potential in breast cancer via binding to ERalpha and activation of the transcriptional activity of ERalpha. PMID: 21946067
  44. 14-3-3 theta is a new and important regulatory protein in the TLR-2 and TLR-4 signaling suppressing the MyD88-dependent pathway PMID: 21827211
  45. The phosphatidylinositol transfer protein RdgBbeta binds 14-3-3 via its unstructured C-terminus, whereas its lipid-binding domain interacts with the integral membrane protein ATRAP (angiotensin II type I receptor-associated protein). PMID: 21728994
  46. Results suggest that 14-3-3 proteins may be associated with the formation of SOD1-containing inclusions, in FALS patients and the mutant SOD1-Tg mice. PMID: 21655264
  47. the toxin fusicoccin promotes binding of regulatory 14-3-3 proteins to glycoprotein Ibalpha and hampers binding to glycoprotein Ibbeta subunit. PMID: 21395556
  48. novel role for 14-3-3tau in the regulation of Beclin 1 expression and autophagy PMID: 20454448
  49. Depletion of Lats2 or 14-3-3gamma by siRNA inhibits P-body formation in response to UV. PMID: 21118956
  50. The study found that the 14-3-3 tau expression level with the formation of syncytiotrophoblast cells increased. PMID: 21046037


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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.

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