Recombinant Mouse Endoribonuclease Zc3H12A (ZC3H12A) Protein (His&Myc)

Name: Recombinant Mouse Endoribonuclease Zc3H12A (ZC3H12A) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05154P
Price: 680.8 USD
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Zc3h12a.

Collections: Chemokines and receptors, Cytokines, Cytokines and growth factors, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Endoribonuclease Zc3H12A (ZC3H12A) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q5D1E7
Target Symbol	ZC3H12A
Synonyms	Zc3h12a; Mcpip; Mcpip1; Endoribonuclease ZC3H12A; EC 3.1.-.-; Monocyte chemotactic protein-induced protein 1; MCP-induced protein 1; MCPIP-1; Regnase-1; Reg1; Zinc finger CCCH domain-containing protein 12A
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MSDPCGTKPVQESNPTMSLWSLEDRHSSQGRPQPDQDPVAKEAPTSELQMKVDFFRKLGYSSSEIHSVLQKLGVQADTNTVLGELVKHGSATERECQALTAPSPQPPLVPRGGSTPKPSTLEPSLPEEDREGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGKKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRTPVKDKSSQRPSPASQSSSVSLEAEPGSLDGKKLGARSSPGPHREGSPQTCAPAGRSLPVSGGSFGPTEWLAHTQDSLPYTSQECLDSGIGSLESQMSELWGVRGGSPGESGPTRGPYAGYHSYGSKVPAAPSFSPFRPAMGAGHFSVPTDYVPPPPTYPSREYWSEPYPLPPPTPVLQEPQRPSPGAGGGPWGRVGDLAKERAGVYTKLCGVFPPHLVEAVMRRFPQLLDPQQLAAEILSYKSQHLSE
Expression Range	1-596aa
Protein Length	Full Length
Mol. Weight	73.0 kDa
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.
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	Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation. Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A. Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR. Self regulates by destabilizing its own mRNA. Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner. Plays a role in the inhibition of microRNAs (miRNAs) biogenesis. Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs. Plays also a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity. Affects the overall ubiquitination of cellular proteins. Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis. Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Prevents stress granules (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock, and energy deprivation. Plays a role in the regulation of macrophage polarization; promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state. May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis. Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway. Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial proinflammatory cytokine production.
Subcellular Location	Nucleus. Cytoplasm. Rough endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic granule. Cytoplasm, P-body.
Protein Families	ZC3H12 family
Database References	KEGG: mmu:230738 STRING: 10090.ENSMUSP00000037172 UniGene: Mm.402
Associated Diseases	Increased expression of ZC3H12A is associated with ischemic heart disease (PubMed:16574901).
Tissue Specificity	Expressed in CD4(+) helper T-cells (at protein level). Highly expressed in macrophages. Expressed in lung, lymph nodes, spleen and thymus. Expressed weakly in heart. Expressed weakly in cardiomyocytes (at protein level). Expressed in spleen, lung, intesti

Gene Functions References

Regnase-1 predominantly regulates mTORC1 signaling. PMID: 30297433
Thus, these data suggest MCPIP1 as a potent host defense against Coxsackievirus B3 infection and viral myocarditis. PMID: 29043433
MCPIP1 overexpression results in modulated levels of 58 miRNAs in adipocytes on day 2 of differentiation. Among them, 30 miRNAs showed significantly reduced levels and 28 showed increased levels in comparison to control. Approximately one third of the modulated miRNAs were not previously reported to be involved in adipocytes differentiation. PMID: 28939056
duodenal Regnase-1 controls the expression of PHD3, which impairs duodenal iron uptake via HIF2alpha suppression. PMID: 28538180
mutations of both Regnase-1 and Roquin in T cells leads to massive lymphocyte activation and increased TH1 cells. In contrast, mutation of either Regnase-1 or Roquin affected T cell activation to a lesser extent than the double mutation, indicating that Regnase-1 and Roquin function nonredundantly in T cells. Regnase-1 is capable of repressing Roquin mRNA. PMID: 29127149
our findings not only demonstrate that MCPIP1 plays an important role in early cortical neurogenesis but also reveal an unexpected link between neocortical development, immune regulators, and epigenetic modification. PMID: 27523618
MCPIP1 is a potent negative regulator of psoriatic skin inflammation through IL-17A and IL-17C PMID: 27920272
IL-17A-mediated induction of MCPIP1 is involved in the regulation of local altered gene expression in suprabasal epidermal layers in psoriasis PMID: 27180111
this study shows that Regnase-1 RNase activity is tightly controlled by both intramolecular and intermolecular interactions PMID: 26927947
Overexpression of MCPIP1 induced apoptosis. PMID: 26833120
MCPIP1 is the target of mmu-miR-27-5p. PMID: 26295043
MCPIP1-MSCs also expressed increased levels of proteins involved in angiogenesis, autophagy, and induction of differentiation PMID: 26214508
This studies demonstrated that MCPIP1 is an important mediator of minocycline-induced protection from brain ischemia. PMID: 25888869
Data indicate that MCPIP1 (also termed Regnase-1, encoded by Zc3h12a) knockdown enhanced interleukin-17 (IL-17)-mediated signaling. PMID: 26320658
MCPIP expression in the ischemic myocardium protects against adverse cardiac remodeling and dysfunction following myocardial infarction PMID: 25840774
both in vivo and in vitro experiments demonstrate that the transcription factors STAT6 and KLF4 implement IL-4-induced M2 polarization via the dual catalytic activities of MCPIP. PMID: 25934862
Findings reveal that differential regulation of mRNAs by Regnase-1 and Roquin depends on their translation status and enables elaborate control of inflammation. PMID: 26000482
Regnase-1 is a key molecule in the regulation of immune responses PMID: 24163394
Roquin inhibited T(H)17 cell differentiation and acted together with the endoribonuclease regnase-1 to repress target mRNA encoding the T(H)17 cell-promoting factors IL-6, ICOS, c-Rel, IRF4, IkappaBNS and IkappaBzeta. PMID: 25282160
MCPIP1 deficiency in mice results in severe anemia related to autoimmune mechanisms. PMID: 24324805
Hematopoietic deficiency of MCPIP1 resulted in severe systemic and multi-organ inflammation but paradoxically diminished atherogenesis in mice. PMID: 24223214
these data confirm that MCPIP1 is a key regulator of adipogenesis. PMID: 24418043
these results suggest a prominent role for MCPIP1 in the control of inflammation and immune homeostasis. PMID: 23567898
MCPIP1 deficiency caused significant lack of electroacupuncture pretreatment-induced cerebral protective effects PMID: 23663236
MCPIP1 selectively suppresses TLR4 signaling pathway and protects mice from LPS-induced septic shock. PMID: 23422584
MCPIP1 is regulated by IL-17 and IL-1 PMID: 23658019
These results indicate that dynamic control of Regnase-1 expression in T cells is critical for controlling T cell activation. Manipulation of Malt1-mediated Regnase-1 expression appears to be an important contrcontrol point for T-cell-mediated immune responses in vivo. PMID: 23706741
MICIP is found in rheumatoid arthritis leading to endothelial dysfunction. PMID: 23580143
these results implicate MCPIP1 as a potent regulator of innate immunity, which can be strongly engaged in the pathogenesis of acute and chronic infective diseases. PMID: 22777400
MCPIP induces adipogenesis via induction of reactive oxygen/nitrogen species that leads to endoplasmic reticulum stress. PMID: 22739135
Data indicate that absence of MCPIP1 exacerbates ischemic brain damage by upregulation of proinflammatory cytokines and that MCPIP1 participates in LPS-induced ischemic stroke tolerance. PMID: 22196138
MCPIP1 coordinates SG formation and apoptosis during cellular stress and may play a critical role in immune homeostasis and resolution of macrophage inflammation. PMID: 21971051
MCPIP has therapeutic values to protect heart from inflammatory pathologies. PMID: 21616078
Data show that MCPIP1 negatively regulates c-Jun N-terminal kinase (JNK) and NF-kappaB activity by removing ubiquitin moieties from proteins, including TRAF2, TRAF3, and TRAF6. PMID: 21115689
MCPIP1, 2, 3, and 4, encoded by four genes, Zc3h12a, Zc3h12b, Zc3h12c, and Zc3h12d, respectively, regulates macrophage activation. PMID: 18178554
results indicate that Zc3h12a is an essential RNase that prevents immune disorders by directly controlling the stability of a set of inflammatory genes PMID: 19322177
MCP-1 (monocyte chemotactic protein-1)-induced protein is a newly identified protein that can induce adipogenesis without PPARgamma. PMID: 19666473
It is a novel RNase and regulates inflammatory responses via regulating the gene expression of mRNA coding IL-6. (review) PMID: 19894584

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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.

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