Recombinant Human Cyclic Amp-Dependent Transcription Factor Atf-2 (ATF2) Protein (His-SUMO)

Name: Recombinant Human Cyclic Amp-Dependent Transcription Factor Atf-2 (ATF2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10004P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Cyclic Amp-Dependent Transcription Factor Atf-2 (ATF2) 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	P15336
Target Symbol	ATF2
Synonyms	Activating transcription factor 2; Activating transcription factor 2 splice variant ATF2 var2; ATF 2; Atf-2; Atf2; ATF2 protein; ATF2_HUMAN; cAMP Response Element Binding Protein 2; cAMP response element binding protein CRE BP1; cAMP response element-binding protein CRE-BP1; cAMP responsive element binding protein 2; formerly; cAMP-dependent transcription factor ATF-2; cAMP-responsive element-binding protein 2; CRE BP1; CRE-BP; CREB 2; CREB-2; CREB2; CREBP1; Cyclic AMP dependent transcription factor ATF 2; Cyclic AMP-dependent transcription factor ATF-2; Cyclic AMP-responsive element-binding protein 2; D130078H02Rik; D18875; HB 16; HB16; Histone acetyltransferase ATF2; MGC105211; MGC105222; MGC111558; MGC142504; mXBP; MXBP protein; Tg(Gzma-Klra1)7Wum; TREB 7; TREB7
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQSTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDISVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPSSQSQPSGS
Expression Range	1-505aa
Protein Length	Full Length
Mol. Weight	70.5kDa
Research Area	Transcription
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	Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type.
Subcellular Location	Nucleus. Cytoplasm. Mitochondrion outer membrane. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mitochondrial outer membrane in response to genotoxic stress. Phosphorylation at Thr-52 is required for its nuclear localization and negatively regulates its mitochondrial localization. Co-localizes with the MRN complex in the IR-induced foci (IRIF).
Protein Families	BZIP family, ATF subfamily
Database References	HGNC: 784 OMIM: 123811 KEGG: hsa:1386 STRING: 9606.ENSP00000264110 UniGene: PMID: 28429654 deregulation of the miR-144-5p/ATF2 axis plays an important role in non-small-cell lung cancer cell radiosensitivity. PMID: 29850528 p38alpha and ATF2 expression play a crucial role in the malignant phenotypes of ovarian tumor cells and are a markers of poor prognosis in patients with ovarian serous adenocarcinomas. PMID: 28916425 activation of JNK was found to be dependent on muscarinic acid receptor induced Ca(2+)/CAMKII as well as ROS. JNK dependent phosphorylation of ATF2/c-Jun transcription factors resulted in TGF-beta transcription and its signaling. PMID: 27708346 ATF2 regulated by miR-204 might also play an important role in the regulation of malignant behavior of glioblastoma. PMID: 27588402 We further demonstrated the suppressive function of lncRNA#32 in hepatitis B virus and hepatitis C virus infection. lncRNA#32 bound to activating transcription factor 2 (ATF2) and regulated ISG expression. Our results reveal a role for lncRNA#32 in host antiviral responses. PMID: 27582466 Results show that ATF2 is highly expressed in renal cell carcinoma (RCC) tissues and promotes RCC cell proliferation, migration and invasion. The study suggests that ATF2 exerts an oncogenic role in RCC. PMID: 27377902 These findings point to an oncogenic function for ATF2 in melanoma development that appears to be independent of its transcriptional activity. PMID: 27210757 this study demonstrates that CPEB2 alternative splicing is a major regulator of key cellular pathways linked to anoikis resistance and metastasis. PMID: 28904175 Noxin facilitated the expression of Cyclin D1 and Cyclin E1 through activating P38-activating transcription factor 2 signaling pathway, thus enhanced cell growth of breast cancer PMID: 28618963 these observations suggest that CD99 is involved in the regulation of CD1a transcription and expression by increasing ATF-2. PMID: 27094031 This review provides an overview of the currently known upstream regulators and downstream targets of ATF2. [review] PMID: 28212892 TNF induces the binding of ATF2 to the TNF-responsive element. PMID: 27821620 miR-204 may act as a tumor suppressor by directly targeting ATF2 in non-small cell lung cancer PMID: 26935060 the variant alleles of TSG101 rs2292179 and ATF2 rs3845744 were associated with a reduced risk of breast cancer, particularly for subjects with BMI <24 (kg/m(2)) and postmenopausal women, respectively PMID: 26729199 Results reveal that mitochondrial ATF2 is associated with the induction of apoptosis and BRAF inhibitor resistance through Bim activation. PMID: 26462148 Neisseria meningitidis caused a high level of E-selectin expression elicited by the activity of phosphorylated ATF2 transcription factor on the E-selectin promoter. PMID: 26153406 increased expression of the gene encoding PKCepsilon and abundance of phosphorylated, transcriptionally active ATF2 were observed in advanced-stage melanomas and correlated with decreased FUK expression PMID: 26645581 CARMA1- and MyD88-dependent activation of Jun/ATF-type AP-1 complexes is a hallmark of ABC diffuse large B-cell lymphomas. PMID: 26747248 More terminally differentiated human odontoblasts was ATF-2 positive, as compared to pulpal fibroblasts at various stages of differentiation: ATF-2 is more associated with cell survival rather than cell proliferation. PMID: 25417007 Study identified a potential target of miR-451, ATF2, and revealed a novel role of miR-451 in the inhibition of the migratory ability of hepatoma cell lines. PMID: 24968707 ATF-2 knockdown blocked VEGF-A-stimulated VCAM-1 expression and endothelial-leukocyte interactions. ATF-2 was also required for other endothelial cell outputs, such as cell migration and tubulogenesis. PMID: 24966171 Study demonstrates the role of miR-622 in suppressing glioma invasion and migration mediated by ATF2, and shows that miR-622 expression inversely correlates with ATF2 in glioma patients PMID: 25258251 suppression of tumorigenesis by JNK requires ATF2. PMID: 25456131 study revealed that, autocrine soluble factors regulate dual but differential role of ATF-2 as a transcription factor or DNA repair protein, which collectively culminate in radioresistance of A549 cells. PMID: 25041846 While expression of ATF-2 is not associated with outcome. PMID: 25141981 The expression of ATF2 in chondrocytes is involved in apoptosis in Kashin-Beck disease. PMID: 23866832 in human HCC tissues, SPTBN1 expression correlated negatively with expression levels of STAT3, ATF3, and CREB2; SMAD3 expression correlated negatively with STAT3 expression PMID: 25096061 zymosan-induced il23a mRNA expression is best explained through coordinated kappaB- and ATF2-dependent transcription; and (iii) il23a expression relies on complementary phosphorylation of ATF2 on Thr-69 and Thr-71 dependent on PKC and MAPK activities. PMID: 24982422 Data show that salvianolic acid B protects endothelial progenitor cells against oxidative stress by modulating Akt/mTOR/4EBP1, p38 MAPK/ATF2, and ERK1/2 signaling pathways. PMID: 24780446 There is synergism between developmental stage-specific recruitments of the ATF2 protein complex and expression of gamma-globin during erythropoiesis. PMID: 24223142 An association between ATF2 polymorphisms and heavy alcohol consumption is only weakly supported. PMID: 24338393 ATF2 knockdown revealed ATF2-triggered p21(WAF1) protein expression, suggesting p21(WAF1) transactivation through ATF2. PMID: 23800081 results therefore suggest that c-MYC induces stress-mediated activation of ATF2 and ATF7 and that these transcription factors regulate apoptosis in response to oncogenic transformation of B cells PMID: 23416976 we establish that ATF2 family members physically and functionally interact with TCF1/LEF1 factors to promote target gene expression and hematopoietic tumor cell growth PMID: 23966864 Cytoplasmic ATF2 expression was less frequently seen than nuclear expression in malignant mesenchymal tumors. Benign mesenchymal tumors mostly showed much lower nuclear and cytoplasmic ATF2 expression. PMID: 24289970 Data indicate that small molecules that block the oncogenic addiction to PKCepsilon signaling by promoting ATF2 nuclear export, resulting in mitochondrial membrane leakage and melanoma cell death. PMID: 23589174 Increasing of ATF2 expression is mediated via oxidative stress induced by arsenic in SV-HUC-1 cells, and MAPK pathways are involved. PMID: 23591579 these studies show that the IL-1beta-induced increase in intestinal tight junction permeability was regulated by p38 kinase activation of ATF-2 and by ATF-2 regulation of MLCK gene activity PMID: 23656735 Phosphorylation of ATF2 by PKCepsilon is the master switch that controls its subcellular localization and function. PMID: 22685333 ATF2-Jun heterodimers bind IFNb in both orientations alone and in association with IRF3 and HMGI PMID: 22843696 we report the kinetic mechanism for JNK1beta1 with transcription factors ATF2 and c-Jun along with interaction kinetics for these substrates. PMID: 22351776 ATF2 subcellular localization is probably modulated by multiple mechanisms PMID: 22275354 Data concluded that IR-induced up-regulation of ATF2 was coordinately enhanced by suppression of miR-26b in lung cancer cells, which may enhance the effect of IR in the MAPK signaling pathway. PMID: 21901137 The ability of ATF2 to reach the mitochondria is determined by PKCepsilon, which directs ATF2 nuclear localization. Genotoxic stress attenuates PKCepsilon effect on ATF2; enables ATF2 nuclear export and localization at the mitochondria. PMID: 22304920 Data show that ATF7-4 is an important cytoplasmic negative regulator of ATF7 and ATF2 transcription factors. PMID: 21858082 Our data suggest regulatory roles for ATF2 in TNF-related mechanisms of Head and Neck Squamous Cell Carcinoma. Its perturbation and nuclear activation are associated with significant effects on survival and cytokine production. PMID: 21990224 Data suggest that competition between GSTpi and active JNK for the substrate ATF2 may be responsible for the inhibition of JNK catalysis by GSTpi. PMID: 21384452 ATF2 interacts with beta-cell-enriched transcription factors, MafA, Pdx1, and beta2, and activates insulin gene transcription. PMID: 21278380 MITF is downregulated by ATF2 in the skin of Atf2-/- mice, in primary human melanocytes, and in melanoma cell lines. PMID: 21203491

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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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