Recombinant Human Protein Cbfa2T1 (RUNX1T1) Protein (His&Myc)

Name: Recombinant Human Protein Cbfa2T1 (RUNX1T1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01983P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Protein Cbfa2T1 (RUNX1T1) 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	Q06455
Target Symbol	RUNX1T1
Synonyms	Cyclin-D-related protein (Eight twenty one protein) (Protein ETO) (Protein MTG8) (Zinc finger MYND domain-containing protein 2)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MISVKRNTWRALSLVIGDCRKKGNFEYCQDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQQGDTPAVSSSVTPNSGAGSPMDTPPAATPRSTTPGTPSTIETTPR
Expression Range	1-604aa
Protein Length	Full Length
Mol. Weight	75 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	Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Can repress transactivation mediated by TCF12. Acts as a negative regulator of adipogenesis. The AML1-MTG8/ETO fusion protein frequently found in leukemic cells is involved in leukemogenesis and contributes to hematopoietic stem/progenitor cell self-renewal.
Subcellular Location	Nucleus. Note=Colocalizes with ATN1 in discrete nuclear dots.
Protein Families	CBFA2T family
Database References	HGNC: 1535 OMIM: 133435 KEGG: hsa:862 STRING: 9606.ENSP00000402257 UniGene: PMID: 28166825 The data suggest that the tumor suppressor activity of both RUNX1t1 and TFF1 are mechanistically connected to CEBPB and that cross-regulation between CEBPB-RUNX1t1-TFF1 plays an important role in gastric carcinogenesis. PMID: 27522676 The role of RUNX1T1 in t(8;21) acute myeloid leukemia and miRNA expression regulation PMID: 28322996 Our data revealed a novel role for RUNX1T1 as a tumor-suppressor gene in colorectal cancer through modulation of multiple cellular pathways affecting the cell cycle, DNA damage, DNA replication, estrogen signaling, and drug resistance PMID: 27798886 A substantial fraction of AML1-ETO/p300 co-localization occurs near TSSs in promoter regions associated with transcriptionally active loci. PMID: 25928846 A reduction in KIT mRNA levels was also observed in AE-silenced cells, but silencing KIT expression reduced cell growth but did not induce apoptosis. PMID: 24727677 RUNX1T1 gene may participate in t(8;21)(q22;q22)-dependent leukemic transformation due to its multiple interactions in cell regulatory network particularly through synergistic or antagonistic effects in relation to activity of RUNX1-RUNX1T1 fusion gene. PMID: 24976338 Runx1t1 epigenetically regulates the proliferation and nitric oxide production of microglia. PMID: 24586690 The cooperative effect of the expression of mutated KIT and AML1-ETO oncogenes is crucial for selective toxic action of binase on malignant cells. PMID: 22101339 RUNX1T1 point mutation may be rare and passenger mutations in acute leukemias, lung and breast cancers PMID: 21571369 SMAD4 knockdown accelerated this re-silencing process, suggesting that normal TGF-beta signaling is essential for the maintenance of RunX1T1 expression PMID: 21540640 Data show that low RUNX1T1 expression was highly associated with hepatic metastases. PMID: 21499216 Elevated levels of AES mRNA and protein were confirmed in AML1/ETO-expressing leukemia cells, as well as in other acute myeloid leukemia specimens. PMID: 21245488 ETO nervy homology region (NHR) 3 domain-PKA(RIIalpha) protein interaction does not appear to significantly contribute to AML1-ETO's ability to induce leukemia. PMID: 20708017 The critical role for an evolutionary conserved GATA binding site in transcriptional regulation of the ETO gene in cells of erythroid/megakaryocytic potential. PMID: 20487545 NHR4 domain mutations of ETO are probably very infrequent in AML1-ETO positive myeloid leukemia cells. PMID: 20090777 no conclusive evidence as yet that the AML1/ETO chimeric gene is sufficient per se to induce leukemia. PMID: 11869944 Analysis of nuclear distribution of the AML1/ETO protein and its homology domains led to identification of domains in ETO responsible for intranuclear transport and subnuclear distribution of AML1/ETO. PMID: 11983111 2 independent subnuclear targeting signals in the N- and C-terminal regions of ETO direct ETO to the same binding sites occupied by AML1ETO. This provides a molecular basis for aberrant subnuclear targeting of AML1ETO, the defect in t(8;21)-related AML. PMID: 12427969 ETO rearrangements leading to the AML1-ETO fusion gene are frequently the result of small hidden interstitial insertions. PMID: 12557226 Data identify ETO as a partner for Gfi-1 and Gfi-1B, and suggest that Gfi-1 proteins repress transcription through recruitment of histone deacetylase-containing complexes. PMID: 12874834 ETO is a bona fide corepressor that links the transcriptional pathogenesis of acute leukemias and B-cell lymphomas and offers a compelling target for transcriptional therapy of hematologic malignancies. PMID: 14551142 RT-PCR for the detection of AML1/ETO in children with acute non-lymphoid leukemia (ANLL) was quick, convenient and sensitive, and could be regarded as a useful method for the diagnosis and prognosis of ANLL. PMID: 14751048 cloning, expression, purification and crystallization of NHR3 domain PMID: 15295650 These findings suggest a central role of RUNX1-CBFA2T1 in the maintenance of the leukaemia. PMID: 15298716 N-CoR utilizes repression domains I and III for interaction and co-repression with ETO PMID: 15377655 DiffeRential expression of the ETO homologues suggests that they may have a potential role in hematopoietic differentiation. PMID: 15676213 Alternative splicing in the AML1-MTG8 fusion gene occurs in leukemia cell lines as well as in cells of leukemia paatients with a(8;21) translocation. PMID: 15723339 Translocations in acute myeloid leukemia (AML) is the t(8;21) is characterized by AML1-MTG8 (ETO) mutation. PMID: 16502583 AML1T1, an alternatively spliced isoform of the t(8;21) transcript, promotes leukemogenesis. PMID: 16892037 The leukemia-associated fusion protein AML1-ETO could aberrantly transactivate the EEN gene through an AML1 binding site. PMID: 16990610 As a result, we identified 14 unique proteins deregulated in AML1-ETO-carrying leukemic cells, including 3 up-regulated such as hairy and enhancer of split 5 (HES5) and 11 down-regulated such as MAT1 (menage a trois-1. PMID: 17058450 AML1/ETO participates in a protein complex with the RA receptor alpha (RARalpha) at RA regulatory regions on RARbeta2. PMID: 17244680 Loss of p21(WAF1) facilitates AML1-ETO-induced leukemogenesis. PMID: 17284535 Isoform AML1/ETO9a was correlated to acute myeloid leukemia-M2 subtype. PMID: 17649722 Our study suggests that KIT activating mutations in AML with t(8; 21) are associated with diminished CD 19 and positive CD56 expression on leukemic blasts and, thus, can be phenotypically distinguished from AML1-ETO leukemias PMID: 17875504 MTG8/ETO and Mtg16 (ETO2) associated with TCF4 PMID: 18039847 These results demonstrate that scl is an important mediator of the ability of AML1-ETO to reprogram hematopoietic cell fate decisions, suggesting that scl may be an important contributor to AML1-ETO-associated leukemia. PMID: 18156164 The interaction between SIN3B and ETO required an intact amino-terminus of ETO and the NHR2 domain. PMID: 18205948 Knockdown of TLE1 or TLE4 levels increased the rate of cell division of the AML1-ETO-expressing Kasumi-1 cell line, whereas forced expression of either TLE1 or TLE4 caused apoptosis and cell death. PMID: 18258796 ETO family member-mediated oligomerization and repression can be distinct events and that interaction between ETO family members and hSIN3B or N-CoR may not necessarily strengthen transcriptional repression. PMID: 18586123 the crucial role of the NHR4 domain in determination of cellular fate during AML1-ETO-associated leukemogenesis. PMID: 18952841 a major role for the functional interaction of AML1/ETO with AML1 and HEB in transcriptional regulation determined by the fusion protein. PMID: 19043539 Four copies of RUNX1T1 were found. PMID: 19100510 Data show that E proteins contain another conserved ETO-interacting region, termed DES, and that differential associations with AD1 and DES allow ETO to repress transcription through both chromatin-dependent and chromatin-independent mechanisms. PMID: 19289505

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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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