Recombinant Human Endoribonuclease Zc3H12A (ZC3H12A) Protein (His)

Name: Recombinant Human Endoribonuclease Zc3H12A (ZC3H12A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00773P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Endoribonuclease Zc3H12A (ZC3H12A) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q5D1E8
Target Symbol	ZC3H12A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE
Expression Range	1-599aa
Protein Length	Full Length
Mol. Weight	69.8 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 granule (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.; (Microbial infection) Binds to Japanese encephalitis virus (JEV) and Dengue virus (DEN) RNAs.; (Microbial infection) Exhibits antiviral activity against HIV-1 in lymphocytes by decreasing the abundance of HIV-1 viral RNA species.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasm, P-body. Rough endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic granule.
Protein Families	ZC3H12 family
Database References	HGNC: 26259 OMIM: 610562 KEGG: hsa:80149 STRING: 9606.ENSP00000362174 UniGene: PMID: 29379093 Data indicate a mechanism used by monocyte chemotactic protein-inducing protein 1 (MCPIP1) to negatively regulated type I IFN interferon-beta antiviral defense. PMID: 29920243 Although interleukin-6 (IL-6) mRNA level was higher in 3D-culured cells, its secretion levels were higher in 2D-cultured cells. In addition, the levels of mRNA and protein expression of regnase-1, regulatory RNase of inflammatory cytokine, significantly increased in 3D culture, suggesting post-translational modification of IL-6 mRNA via regnase-1. PMID: 30096769 The activation of p38 in response to low doses of ultraviolet radiation was postulated to be protective for p53-inactive cells. Therefore, MCPIP1 may favor the survival of p53-defective HaCaT cells by sustaining the activation of p38. PMID: 29103983 Conclusively, these data demonstrate the MCPIP1 contributes to attenuate influenza A virus-induced host antiviral response by suppressing RIG-I expression. PMID: 28892164 MCPIP1 contributes to the clear cell renal cell carcinoma development. PMID: 28197812 MCPIP1 is an important positive regulator of IFNs antiviral activity. PMID: 29545178 MCPIP1 contributes to the UVB response of keratinocytes by altering metabolic and apoptotic processes and the release of inflammatory mediators. PMID: 28377026 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 A comprehensive update on the function, regulation and molecular mechanisms of Regnase-1 is provided. Authors propose that Regnase-1 may function as a master rapid response gene for cellular adaption triggered by microenvironmental changes. [Review] PMID: 28194024 Regnase-1 controls the magnitude of innate and adaptive immune responses, and thereby dysfunction of this protein in mice leads to the development of spontaneous systemic inflammation. PMID: 28475459 data extend knowledge on roles of MCPIP1 in our model and link the protein to regulation of expression and stability of MYCN through decrease of signaling via Akt/mTOR pathway. PMID: 27935099 Loss of MCPIP1 expression is associated with Clear Cell Renal Cell Carcinoma metastasis. PMID: 28716897 this study uncovered a novel IL-8-dependent mechanism via which MCPIP-1 maintains epithelial homeostasis PMID: 27513529 These data revealed that influenza A virus-induced expression of miR-9 negatively regulated MCPIP1 expression and partially acts as a brake on host MCPIP1-mediated antiviral effect. PMID: 27322373 MCPIP1 recognizes regions of the 3'UTR of C/EBPbeta mRNA. PMID: 28328949 MCPIP1 is a potent negative regulator of psoriatic skin inflammation through IL-17A and IL-17C PMID: 27920272 SAHA-mediated suppression of the IL-6 expression is achieved through increased recruitment of CEBPalpha to the MCPIP1 promoter and by relieving the miR-9-mediated inhibition of MCPIP1 expression in OA chondrocytes. PMID: 27404795 IL-17A-mediated induction of MCPIP1 is involved in the regulation of local altered gene expression in suprabasal epidermal layers in psoriasis PMID: 27180111 propose that KSHV infection inhibits a negative regulator of miRNA biogenesis (MCPIP1) and up-regulates critical miRNA processing components to evade host mechanisms that inhibit expression of viral miRNAs PMID: 27893764 both human and cynomolgus monkey MCPIP1 restrict simian immunodeficiency virus replication. Unlike SAMHD1, MCPIP1-mediated HIV-1 restriction cannot be overcome by SIV Vpx. PMID: 27075251 Regnase-1 can be induced by HMGB1 in microglia and negatively regulates HMGB1-mediated neuroinflammation and neuronal toxicity PMID: 27044405 findings provide novel insight into the potential targeting of MCPIP1 or autophagy in the development of potential therapeutic strategies for silicosis PMID: 27782836 These findings reveal a new potential function of MCPIP1, suggesting a possible mechanism of fibrosis in pulmonary silicosis. PMID: 27866190 The human conserved stem-loop structure is not sufficient for ZC3H12A-dependent degradation. PMID: 27494113 expression of miR-3613-3p might be regulated by MCPIP1 by cleavage of its precursor form. PMID: 26308737 Suggest that MCPIP1 may play an important role in cholesterol induced damage in endothelial cells. PMID: 26617772 Findings show increased MCP1P expression in a model of Ischemia/Reperfusion Injury (I/R) and suggest a vital role for MCPIP1 in cell migration and apoptosis, resulting in increased angiogenesis and apoptosis during the late stages of I/R. PMID: 26329288 In white blood cells from patients with SLE, MCPIP1 expression was elevated, and its expression correlated positively with the IFN score and negatively with the miR-146a transcript level. PMID: 26315540 demonstrated induction of MCPIP1 in human fibroblasts embedded in the stress-released 3-D collagen matrix, which occurred through activation of mitogen-activated protein kinases, phosphoinositide 3-kinase, and NF-kappaB PMID: 26399696 In this review we summarize current progress regarding the specific characteristics of sequences and structures in the 3' untranslated regions of mRNAs that are recognized by tristetraproline, Roquins, and Regnase-1. PMID: 25955820 miR-139-mediated downregulation of MCPIP1 promotes IL-6 expression in osteoarthritis. PMID: 26450708 MCPIP1 and MCPIP4 form a complex but they act independently in regulation of IL-6 mRNA degradation. PMID: 26134560 Data show that regulator of G protein signaling 2 (RGS2) was stabilized by deubiquitinase monocyte chemotactic protein-induced protein 1 (MCPIP1). PMID: 25187114 MCPIP1 may suppress hepatitis C virus replication and hepatitis C virus-mediated proinflammatory responses with infection, which might contribute to the regulation of host defense against the infection and virus-induced inflammation. PMID: 25225661 MCPIP1-associated USP10 is essential for negative regulation of NF-kappaB activation. PMID: 24270572 MCPIP1 acts as an RNase to limit HIV-1 production in resting CD4+ T cells. PMID: 24191027 The present results show for the first time that the antidicer RNase activity of MCPIP1 is critical in mediating the angiogenic function of MCPIP. PMID: 24048733 These results demonstrate that MCPIP may be an important regulator of inflammatory angiogenesis and provide novel mechanistic insights into the link between MCP-1 and cardiovascular diseases. PMID: 24008336 MCPIP1 is regulated by IL-17 and IL-1 PMID: 23658019 Taken together, these data demonstrate that MCPIP1 down-regulates via an ARE-independent pathway PMID: 23185455 MCPIP1 can act as a host innate defense via RNase activity for targeting and degrading viral RNA. PMID: 23355615 MCPIP-induces differentiation via induction of oxidative stress that leads to ER stress that causes autophagy involved in tube formation. PMID: 22820500 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 Our data suggest that Zc3h12a is a novel IL-6 regulator in fibroblast-like synovial cells, which may be involved in the progression of rheumatoid arthritis. PMID: 22132693 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 MCPIP1 ribonuclease antagonizes dicer and terminates microRNA biogenesis through precursor microRNA degradation. PMID: 22055188 REVIEW: Understanding ZC3H12A gives a comprehensive panorama that promises to improve our understanding of processes in which this gene is involved including autoimmune, infectious and cardiovascular diseases. PMID: 20807520 May cause cell death and plays important role in development of ischemic heart disease. Could be a potential target for therapeutic intervention. PMID: 16574901 MCPIP1, 2, 3, and 4, encoded by four genes, Zc3h12a, Zc3h12b, Zc3h12c, and Zc3h12d, respectively, regulates macrophage activation. PMID: 18178554

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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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