Recombinant Human Runt-Related Transcription Factor 1 (RUNX1) Protein (His&Myc)

Name: Recombinant Human Runt-Related Transcription Factor 1 (RUNX1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06120P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Runt-Related Transcription Factor 1 (RUNX1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q01196
Target Symbol	RUNX1
Synonyms	Acute myeloid leukemia 1; Acute myeloid leukemia 1 protein; alpha subunit core binding factor; AML 1; AML1; AML1 EVI 1; AML1 EVI 1 fusion protein; Aml1 oncogene; AMLCR 1; AMLCR1; CBF alpha 2; CBF-alpha-2; CBFA 2; CBFA2; Core binding factor alpha 2 subunit; Core binding factor runt domain alpha subunit 2; Core-binding factor subunit alpha-2; EVI 1; EVI1; HGNC; Oncogene AML 1; Oncogene AML-1; OTTHUMP00000108696; OTTHUMP00000108697; OTTHUMP00000108699; OTTHUMP00000108700; OTTHUMP00000108702; PEA2 alpha B; PEA2-alpha B; PEBP2 alpha B; PEBP2-alpha B; PEBP2A2; PEBP2aB; Polyomavirus enhancer binding protein 2 alpha B subunit; Polyomavirus enhancer-binding protein 2 alpha B subunit; Run1; Runt related transcription factor 1; Runt-related transcription factor 1; RUNX 1; Runx1; RUNX1_HUMAN; SL3 3 enhancer factor 1 alpha B subunit; SL3-3 enhancer factor 1 alpha B subunit; SL3/AKV core binding factor alpha B subunit; SL3/AKV core-binding factor alpha B subunit
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEEAVWRPY
Expression Range	1-453aa
Protein Length	Full Length
Mol. Weight	53.8 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.
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	Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. Essential for the development of normal hematopoiesis. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-dependent transcriptional activation. Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing. Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells. Positively regulates the expression of RORC in T-helper 17 cells.; Isoform AML-1G shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation.; Isoform AML-1L interferes with the transactivation activity of RUNX1.
Subcellular Location	Nucleus.
Database References	HGNC: 10471 OMIM: 151385 KEGG: hsa:861 STRING: 9606.ENSP00000300305 UniGene: PMID: 29778230 Results show that Runx1 associates with c-Abl kinase through its C-terminal inhibitory domain which directly binds to c-Abl. Also, Runx1 is phosphorylated by c-Abl kinase modulating its transcriptional activity and megakaryocyte maturation. PMID: 29730354 DEGs and pathways identified in the present study will help understand the molecular mechanisms underlying RUNX1 mutations in AML and develop effective therapeutic strategies for RUNX1-mutation AML. PMID: 30289875 RUNX1 regulates ITGA6 through a consensus RUNX1 binding motif in its promoter PMID: 28926098 Loss of RUNX1 resulted in enhanced proliferation, migration, and invasion of lung adenocarcinomas PMID: 28926105 Ezh2 and Runx1 mutations collaborate to initiate lympho-myeloid leukemia in early thymic progenitors PMID: 29438697 miR-144 mimics can inhibit the proliferation and migration of ovarian cancer cells though regulating the expression of RUNX1. PMID: 29445078 The effect of FENDRR on cell proliferation, apoptosis and invasion and migration ability in protate cancer cells was suppressed by silence of RUNX1. PMID: 29465000 KSRP, miR-129, and RUNX1 participate in a regulatory axis to control the outcome of myeloid differentiation. PMID: 29127290 PKM2 as a novel target of RUNX1-ETO and is specifically downregulated in RUNX1-ETO positive AML patients, indicating that PKM2 level might have a diagnostic potential in RUNX1-ETO associated AML. PMID: 28092997 specific type of RUNX1 mutation did not affect its association pattern with trisomy 21 PMID: 29249799 High RUNX1 expression is associated with prostatic cancer. PMID: 29328406 RUNX1 Mutation is associated with acute myeloid leukemia. PMID: 29479958 The specific association of ZBTB7A mutations with t(8;21) rearranged acute myeloid leukaemia points towards leukemogenic cooperativity between mutant ZBTB7A and the RUNX1/RUNX1T1 fusion protein has been reported. PMID: 27252013 miR-216a-3p can promote gastric cancer cell proliferation, migration, and invasion via targeting RUNX1 and activating the NF-kappaB signaling pathway PMID: 28835317 the t(5;21)(p15;q22) translocation could be identified only when what had seemed like a del(21)(qq) in G-banded preparations was examined using FISH and RNA-sequencing directed at finding out what lay behind the 21q-. PMID: 29672642 Our findings show the profound impact of RUNX1 allele dosage on gene expression profile and glucocorticoid sensitivity in AML, thereby opening opportunities for preclinical testing which may lead to drug repurposing and improved disease characterization. PMID: 28855357 This study established inducible RUNX1b/c-overexpressing human embryonic stem cell (hESC) lines, in which RUNX1b/c overexpression prevented the emergence of CD34+ cells from early stage, thereby drastically reducing the production of hematopoietic stem/progenitor cells. Simultaneously, the expression of hematopoiesis-related factors was downregulated. PMID: 28992293 Genome-engineered hPSCs expressing ETV6-RUNX1 from the endogenous ETV6 locus show expansion of the CD19(-)IL-7R(+) compartment PMID: 29290585 our study demonstrated that specific bone marrow abnormalities and acquired genetic alterations may be harbingers of progression to hematological malignancies in patients with familial platelet disorder with germline RUNX1 mutation. PMID: 28659335 These studies provide the first evidence in patients with a RUNX1 mutation for a defect in AH (lysosomal) secretion, and for a global defect in secretion involving all three types of platelet granules that is unrelated to a granule content deficiency. They highlight the pleiotropic effects and multiple platelet defects associated with RUNX1 mutations. PMID: 28662545 Younger mRUNX1 AML patients treated with intensive chemotherapy experienced inferior treatment outcomes. In older patients with AML treated with hypomethylating agent (HMA) therapy, response and survival was independent of RUNX1 status. Older mRUNX1 patients with prior myelodysplastic syndrome or myeloproliferative neoplasms (MDS/MPN) had particularly dismal outcome PMID: 28933735 Data indicate miR-29b-1 as a regulator of the AML1-ETO protein (RUNX1-RUNX1T1), and that miR-29b-1 expression in t(8;21)-carrying leukemic cell lines partially rescues the leukemic phenotype. PMID: 28611288 EBPA and RUNX1 are expressed at higher levels in patients with acute myeloid leukemia in comparison to healthy subjects PMID: 28895127 The first characterization of this CASC15 in RUNX1-translocated leukemia. PMID: 28724437 Altogether, these results revealed an unexpected and important epigenetic mini-circuit of AML1-ETO/THAP10/miR-383 in t(8;21) acute myeloid leukaemia, in which epigenetic suppression of THAP10 predicts a poor clinical outcome and represents a novel therapeutic target. PMID: 28539478 Several studies addressed the mechanism by which ETV6/RUNX1 (E/R) contributes to leukemogenesis, including the necessary secondary genetic lesions, the cellular framework in which E/R initially arises and the maintenance of a pre-leukemic condition. [review] PMID: 28418909 MLD- and MLD+ RUNX1-mutated AML differ in some associations to genetic markers, such as +13 or IDH2 mutation status without prognostic impact in multivariate analysis. However, in RUNX1-mutated AML, the overall pattern shows a specific landscape with high incidences of trisomies (such as +8 and +13), and mutations in the spliceosome and in chromatin modifiers PMID: 27211269 RUNX1-RUNX1T1 transcript levels were measured in bone marrow samples collected from 208 patients at scheduled time points after transplantation.Over 90% of the 175 patients who were in continuous complete remission had a >/=3-log reduction in RUNX1-RUNX1T1 transcript levels from the time of diagnosis at each time point after transplantation and a >/=4-log reduction at >/=12 months. PMID: 28166825 RUNX1 defects causing haploinsufficiency are thought to be associated with a lower incidence of myeloid malignancies when compared to those patients with dominant-negative RUNX1 defects. PMID: 28277065 This result suggests that TET2(P1962T) mutation in association with germline RUNX1(R174Q) mutation leads to amplification of a haematopoietic clone susceptible to acquire other transforming alterations PMID: 27997762 Presence of fusion the genes BCR/ABL1, ETV6/RUNX1, and MLL/AF4 does not have any impact on the clinical and laboratory features of ALL at presentation. PMID: 26856288 ETV6/RUNX1 (+) ALL may be heterogeneous in terms of prognosis, and variables such as MRD at end ofremission induction or additional structural abnormalities of 12p could define a subset of patients who are likely to have poor outcome. PMID: 27506214 High RUNX1 expression is associated with lymphoma. PMID: 27056890 PLDN is a direct target of RUNX1 and its dysregulation is a mechanism for platelet dense granule deficiency associated with RUNX1 haplodeficiency PMID: 28075530 The here presented transcriptomic subgroup-based approach unified the gene expression profiles of RUNX1-CBFA2T3 and RUNX1-RUNX1T1 acute myeloid leukemia. PMID: 26968532 Platelet CD34 expression and alpha/delta-granule abnormalities in GFI1B- and RUNX1-related familial bleeding disorders. PMID: 28096094 We observed a strong correlation between EVI1 and alpha1, 6-fucosyltransferase (FUT8) in the chronic phase of the disease and both of them were found to be up-regulated with the progression of the disease. PMID: 27967290 A novel function of RUNX1 and offer an explanation for the link between RUNX1 mutations and chemotherapy and radiation resistance. Moreover, these data suggest that pharmacologic modulation of RUNX1 might be an attractive new approach to treat hematologic malignancies. PMID: 29055018 high EVI1 expression might predict high risk of relapse in AML patients undergoing myeloablative allo-HSCT in CR1. PMID: 27042849 Hypermethylation of the CTNNA1 promoter was associated with unfavorable karyotype, and possessed the higher frequency of coexisting with ASXL1 and RUNX1 mutations. PMID: 27129146 Three siblings with germline causative RUNX1 variant, developed acute myelomonocytic leukemia and acquired variants within the JAK-STAT pathway, specifically targeting JAK2 and SH2B3. PMID: 28513614 These findings suggest RUNX1high is a prognostic biomarker of unfavorable outcome in cytogenetically normal acute myeloid leukemia PMID: 26910834 3 di ff erent heterozygous mutations segregated with thrombocytopenia in 3 families: one missense (c.578T > A/p.Ile193Asn) variant a ff ecting a well conserved residue of the runt-homologous domain, 2 nucleotide substitutions of the canonical "gt" dinucleotide in the donor splice sites of intron 4, (c.351 1 1G > A) and intron 8 (c.967 1 2_5del), and 2 alternative spliced products affecting the transactivation domain. PMID: 28240786 Here, we report the first identification of H3(K27M) and H3(K27I) mutations in patients with AML. We find that these lesions are major determinants of reduced H3K27me2/3 in these patients and that they are associated with common aberrations in the RUNX1 gene. PMID: 28855157 NPM1 mutation but not RUNX1 mutation or multilineage dysplasia defines a prognostic subgroup within de novo acute myeloid leukemia lacking recurrent cytogenetic abnormalities PMID: 28370403 phenotype and bleeding risks of an inherited platelet disorder in a family with a RUNX1 frameshift mutation PMID: 28181366 ERG, FLI1, TAL1, and RUNX1 bind at all AML1-ETO-occupied regulatory regions, including those of the AML1-ETO gene itself, suggesting their involvement in regulating AML1-ETO expression levels. PMID: 27851970 Our work sheds light on the role of RUNX1 and the importance of dosage balance in the development of neural phenotypes in DS. PMID: 27618722 Studies showed a transient expression of RUNX1 during early mesendodermal differentiation of hESCs suggesting it contribution to differentiation in addition to the hematopoietic lineage identity. RUNX1 has a defined role in the epithelial to mesenchymal transition, and the associated competency for cell mobility and motility required for development of the mesendodermal germ layer. [review] PMID: 27591551

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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.

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