Product Details

Purity

>85% (SDS-PAGE)

Target Names

Zfp36

Uniprot No.

P22893

Alternative Names

Zfp36; Nup475; Tis11; Tis11a; Ttp; mRNA decay activator protein ZFP36; Growth factor-inducible nuclear protein NUP475; TPA-induced sequence 11; Tristetraprolin; Zinc finger protein 36; Zfp-36

Species

Mus musculus (Mouse)

Expression Region

1-319

Target Protein Sequence

MDLSAIYESL QSMSHDLSSD HGGTESLGGL WNINSDSIPS GVTSRLTGRS TSLVEGRSCG WVPPPPGFAP LAPRPGPELS PSPTSPTATP TTSSRYKTEL CRTYSESGRC RYGAKCQFAH GLGELRQANR HPKYKTELCH KFYLQGRCPY GSRCHFIHNP TEDLALPGQP HVLRQSISFS GLPSGRRSSP PPPGFSGPSL SSCSFSPSSS PPPPGDLPLS PSAFSAAPGT PVTRRDPNQA CCPSCRRSTT PSTIWGPLGG LARSPSAHSL GSDPDDYASS GSSLGGSDSP VFEAGVFGPP QTPAPPRRLP IFNRISVSE

Protein Length

Full length protein

Tag Info

Tag type will be determined during the manufacturing process.

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
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

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/-80°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.

Target Background

Function

Zinc-finger RNA-binding protein that destabilizes numerous cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation. Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs. Self regulates by destabilizing its own mRNA. Binds to 3'-UTR ARE of numerous mRNAs and of its own mRNA. Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages. Plays also a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response. Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia. Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA. Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA. Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs. Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs. May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro. Involved in the delivery of target ARE-mRNAs to processing bodies (PBs). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing. Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages. Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion. Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis. Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells.

Gene References into Functions

mRNA-binding protein tristetraprolin (TTP) is induced by iron deficiency and degrades mRNAs of mitochondrial Fe/S-cluster-containing proteins, specifically Ndufs1 in complex I and Uqcrfs1 in complex III, to match the decrease in Fe/S-cluster availability. PMID: 29915044
Expression of the RNA-binding protein, tristetraprolin (TTP) was down-regulated in response to calcineurin inhibition. PMID: 29723192
by utilizing Ttp-/- mice we demonstrated the in vivo anti-inflammatory role of Ttp in radiation pneumonitis. PMID: 28548957
Results suggest that RNA-binding proteins such as TTP are expressed and perhaps involved in the modulation of inflammation-induced pregnancy pathologies. PMID: 27732963
The authors found that the endogenous Zfp36 directly interacts with the cytoplasmic poly(A)-binding protein. Importantly, this interaction is required for the translational repression of Zfp36's target mRNAs in resolving inflammation. PMID: 28635594
degrades p28 to inhibit IL-27 production by macrophages and is thereby a negative regulator of the antitumour response PMID: 29021521
Results suggest that tristetraprolin (TTP) as a cytoskeletal regulator is required for spindle morphology/chromosome alignment and actin polymerization in oocytes. PMID: 27458159
RAS signaling can upregulate tumor cell PD-L1 expression through a mechanism involving increases in PD-L1 mRNA stability via modulation of the AU-rich element-binding protein tristetraprolin. PMID: 29246442
these data support the hypothesis that TTP plays a role in the post-transcriptional regulation of the ODC mRNA transcript. PMID: 27193233
Posttranscriptional gene regulation by TTP schedules the termination of the antimicrobial engagement of neutrophils. PMID: 28504646
the gain-of-function mutation of TTP impairs IL-10-mediated negative feedback control of macrophage function in vitro. PMID: 28265004
Studies indicate that mice lacking tristetraprolin (TTP) developed a spontaneous and pervasive inflammatory syndrome. PMID: 27911715
study uncovers a role of TTP as a suppressor of feedback inhibitors of inflammation and highlights the importance of fine-tuned TTP activity-regulation by MK2 in order to control the pro-inflammatory response PMID: 27220464
TTP is not involved in LPS-mediated destabilization of PLCbeta-2 mRNA in macrophages PMID: 28124257
Zinc Finger Protein 36 deficiency has profound effects on the splenic transcriptome. PMID: 26976640
Regulation of mRNAs by tristetraprolin appears to function as one of several critical post-transcriptional regulatory mechanisms controlling satellite cell homeostasis. PMID: 25815583
Tristetraprolin limits inflammatory cytokine production in tumor-associated macrophages in an mRNA decay-independent manner. PMID: 26183929
Dominant suppression of inflammation can be achieved via targeted mutation of the mRNA destabilizing protein tristetraprolin. PMID: 26002976
DUSP1 and tristetraprolin cooperate to regulate macrophage responses to lipopolysaccharide. PMID: 26019272
data shows TTP not only regulates the primary cellular response to innate immune stimuli, exemplified by TNF elaborated from macrophages, but also regulates expression of transcripts involved in the secondary response of mesenchymal cells to TNF stimulation PMID: 25657290
study provides a novel mechanism for the posttranscriptional regulation of TF expression, indicating that this is selectively regulated by PARP-14. PMID: 25293769
Intermedin attenuates macrophage foam-cell formation via tristetraprolin-mediated degradation of CD36 mRNA. PMID: 24253523
Results demonstrate that tristetraprolin acts as a negative regulator of IL-23 gene expression in mouse colon cancer cells and suggest its potential application as a novel therapeutic target to control IL-23-mediated tumor promotion. PMID: 24292977
our study reveals a novel pathway through which TTP suppresses IL-12 production in macrophages, resulting in suppression of Th1 cell differentiation. PMID: 23997224
Tight control of IL23 mRNA stability by TTP is critical to avoid severe inflammation. PMID: 23940256
Enhancing Zinc finger protein 36 expression in vascular endothelial cells, may attenuate atherosclrosis. PMID: 23559629
lactogenesis enhances Tristetraprolin expression PMID: 22968621
this study provided a detailed genetic roadmap for further understanding the regulatory effect of TTP in inflammatory pathways related to human diseases. PMID: 22995314
TTP-driven HIF-1alpha mRNA stabilization is crucial for cell migration. PMID: 22918951
MKP-1 suppressed Tristetraprolin expression by inhibiting p38 MAPK pathway. PMID: 23030431
tristetraprolin inhibits poly(A) tail synthesis by interacting with poly(A)-binding protein nuclear 1 in the nucleus to regulate expression of AU-rich element-containing mRNA PMID: 22844456
Expression of IL-10 is regulated posttranscriptionally by RNA-binding protein tristetraprolin (TTP), which destabilizes IL-10 mRNA in activated macrophages. PMID: 22865915
Myeloid cell TTP plays a critical role in protecting mice against lipopolysaccharide (LPS)-induced septic shock. PMID: 22491258
Data show that acetylcholine regulates muscle inflammation and cell survival, and point to Tristetraprolin and the choice of Mcl-1 mRNA polyadenylation sites as potential key players in muscle reactions to insults. PMID: 22093924
a novel function of TTP in repressing AU-rich mRNA translation PMID: 22203041
downregulates IL-6 gene expression at the post-transcriptional level by targeting AU-rich elements in the 3'UTR region PMID: 21457063
Data show that deletion of TTP completely abolishes IFN-gamma-mediated p19 mRNA degradation. PMID: 21515794
TTP is a master regulator of cytokine expression during homeostasis: without TTP, basal levels of inflammatory cytokines are left unchecked, and their increased production stimulates granulocyte production by committed progenitors entering the cell cycle. PMID: 21270394
MK2 phosphorylation reduces the ability of TTP to promote deadenylation by inhibiting the recruitment of CAF1 deadenylase in a mechanism that does not involve sequestration of TTP by 14-3-3. PMID: 20595389
The RNA binding protein tristetraprolin influences the activation state of murine dendritic cells. PMID: 19945750
TTP is expressed in response to muscle damage, precedes that of MyoD, and is detected 30 minutes after injury. The location of TTP in injured muscle suggests expression by satellite cells. PMID: 12077361
conclude that the physiological functions of TTP depend upon multiple regions of the TTP protein, that TTP has diverged functionally from TIS11b and TIS11d, and that modulation of TNFalpha responses may be a unique and important aspect of TTP function PMID: 12082611
The three-dimensional solution structure of the first domain of Nup475 has been determined by multidimensional nuclear magnetic resonance spectroscopy, revealing a novel fold around a central zinc ion. PMID: 12515557
TTP can be phosphorylated by JNK as well as by the other members of the greater MAP kinase family PMID: 12646273
induction by interleukin-4-stat6 signaling PMID: 14638848
tristetraprolin is phosphorylated by MAPKAP kinase 2 on in vivo sites including Ser178 PMID: 14688255
appears to be a low abundance, cytosolic protein in unstimulated cells and tissues, but once induced is relatively stable, in contrast to its very labile mRNA PMID: 15010466
mechanism by which the p38-MAPK/MAPKAP kinase-2 kinase cascade inhibits TTP-mediated degradation of AU-rich element-containing transcripts PMID: 15014438
stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 and by tristetraprolin itself PMID: 15187092
Review. TTP-deficiency syndrome, its possible genetic modifiers, & the TTP-binding site in TNF-alpha & GM-CSF mRNAs are reviewed. The structure of the complex between RNA & one of the TTP-related proteins is used to model the TTP-RNA binding complex. PMID: 15535838

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Subcellular Location

Nucleus. Cytoplasm. Cytoplasmic granule. Cytoplasm, P-body.

Tissue Specificity

Expressed in skeletal muscle satellite cells. Strongly expressed in differentiated adipocytes compared to preadipocytes (at protein level). Expressed in embryonic stem cells (ESCs). Expressed in heart, placenta, kidney, intestine, liver, lung, thymus, fat

Database Links

KEGG: mmu:22695

STRING: 10090.ENSMUSP00000057815

UniGene: Mm.389856

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Code	CSB-YP026448MO
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Code	CSB-MP026448MO
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Recombinant Mouse Tristetraprolin (Zfp36)

Product Details

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