Recombinant Mouse 14-3-3 Protein Zeta/Delta (YWHAZ) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04140P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse 14-3-3 Protein Zeta/Delta (YWHAZ) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-04140P
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Product Overview

Description Recombinant Mouse 14-3-3 Protein Zeta/Delta (YWHAZ) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P63101
Target Symbol YWHAZ
Synonyms Ywhaz14-3-3 protein zeta/delta; Protein kinase C inhibitor protein 1; KCIP-1; SEZ-2
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN
Expression Range 1-245aa
Protein Length Full Length
Mol. Weight 43.8kDa
Research Area Others
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 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. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation. In neurons, regulates spine maturation through the modulation of ARHGEF7 activity.
Subcellular Location Cytoplasm. Melanosome.
Protein Families 14-3-3 family
Database References

KEGG: mmu:22631

STRING: 10090.ENSMUSP00000022894

UniGene: PMID: 28494163

  • These results demonstrate that miR-146a enhances class switch and secretion of IgE in B cells by upregulating 14-3-3sigma expression, and suggest that miR-146a may be a potential target for asthma therapy. PMID: 29101850
  • When taken together these findings demonstrate novel roles of 14-3-3zeta in the regulation of glucose homeostasis and suggest that modulating 14-3-3zeta levels in intestinal L cells may have beneficial metabolic effects through GLP-1-dependent mechanisms. PMID: 27167773
  • Results indicate that HuR induces 14-3-3zeta translation via interaction with its 3' UTR and that 14-3-3zeta is necessary for stimulation of intestinal epithelial cell migration after wounding. PMID: 27401462
  • PKCdelta-mediated phosphorylation of 14-3-3zeta contributes to the nuclear retention of FOXO1, even when FOXO1 is phosphorylated as under non-stress conditions PMID: 26363783
  • 14-3-3zeta deficient mice in the BALB/c background display behavioral and anatomical defects associated with Schizophrenia-like disorder. PMID: 26207352
  • Ywhaz coordinates adipogenesis in visceral fat. PMID: 26220403
  • An essential role for 14-3-3 zeta in the regulation of macropinocytosis in macrophages upon cytokine stimulation through modulation of the localization of coronin 1. PMID: 25645340
  • In the majority of NAFLD treatment groups and time points the most stable gene was YWHAZ. PMID: 22583519
  • By preventing the inactivation of cofilin, metabolic stress-induced degradation of 14-3-3zeta promotes the conversion of blood monocytes into a hypermigratory, proatherogenic phenotype. PMID: 24812321
  • 14-3-3zeta KO mice displayed enhanced locomotor hyperactivity induced by the dopamine (DA) releaser amphetamine. Consistent with 14-3-3zeta having a role in DA signalling, we found increased levels of DA in the striatum of 14-3-3zeta KO mice. PMID: 24301645
  • The activated serine/threonine kinase Akt/protein kinase B phosphorylated BTK on two sites prior to 14-3-3 zeta binding. PMID: 23754751
  • studies demonstrate that increased 14-3-3zeta levels protect against ER stress and seizure-damage despite down-regulation of the unfolded protein response PMID: 23359526
  • Multiple tumor-associated microRNAs modulate the survival and longevity of dendritic cells by targeting YWHAZ and Bcl2 signaling pathways. PMID: 23355742
  • 14-3-3 zeta as the only prognosticator of local recurrence-free survival (LRFS) and also an independently predicted factor of disease-specific survival (DSS). PMID: 21322651
  • results suggest that 14-3-3zeta, a novel direct binding partner of the L1ICD, promotes L1 phosphorylation by CKII in the central nervous system, and regulates neurite outgrowth, an important biological process triggered by L1 PMID: 20976158
  • Mutation of the 14-3-3 zeta phosphorylation sites in Smad3 markedly reduced the 14-3-3-zeta-mediated inhibition of TGF-beta1-induced p15 promoter-reporter activity & cell cycle arrest in mammary epithelial cells. PMID: 20082218
  • an essential role of 14-3-3zeta as a mediator of the proerythroid differentiation actions of miR-451 PMID: 20679397
  • in miR-144/451(-/-) erythroblasts, 14-3-3zeta accumulates, causing partial relocalization of FoxO3 from nucleus to cytoplasm with dampening of its transcriptional prog PMID: 20679398
  • 14-3-3zeta controls CCTalpha nuclear import in response to calcium signals, thereby regulating mammalian phospholipid synthesis. PMID: 20007511
  • 14-3-3 binds to phosphorylated Raf-1, blocking Raf-1 recruitment to the plasma membrane and preventing its activation PMID: 12801936
  • 14-3-3zeta has a role in MAPKAPK2-mediated phosphorylation, which may represent a novel pathway mediating p38 MAPK-dependent inflammation PMID: 12861023
  • dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface PMID: 12865427
  • 14-3-3 was identified as a binding partner of MITF in osteoclast precursors, and overexpression of 14-3-3 in a transgenic model resulted in increased cytosolic localization of MITF and decreased expression of MITF target genes [14-3-3 zeta] PMID: 16822840
  • 14-3-3:Shc scaffolds can act as multivalent signaling nodes for the integration of both phosphoserine/threonine and phosphotyrosine pathways to regulate specific cellular responses. PMID: 19218246
  • Caspase-2 phosphorylated at S135 binds 14-3-3zeta, thus preventing C2 dephosphorylation. PMID: 19531356

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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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