Recombinant Mouse Transcription Factor Pu.1 (SPI1) Protein (His&Myc)

Name: Recombinant Mouse Transcription Factor Pu.1 (SPI1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00483P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Transcription Factor Pu.1 (SPI1) 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	P17433
Target Symbol	SPI1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MLQACKMEGFSLTAPPSDDLVTYDSELYQRPMHDYYSFVGSDGESHSDHYWDFSAHHVHNNEFENFPENHFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHTGLSHQVSYMPRMCFPYQTLSPAHQQSSDEEEGERQSPPLEVSDGEADGLEPGPGLLHGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRLPPH
Expression Range	1-272aa
Protein Length	Full Length
Mol. Weight	38.8 kDa
Research Area	Others
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	Binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. This protein is a transcriptional activator that may be specifically involved in the differentiation or activation of macrophages or B-cells. Also binds RNA and may modulate pre-mRNA splicing.
Subcellular Location	Nucleus.
Protein Families	ETS family
Database References	KEGG: mmu:20375 STRING: 10090.ENSMUSP00000002180 UniGene: PMID: 29386516 Mice lacking both PU.1 and SpiB in mature B cells do not generate germinal centers and high-affinity antibody after protein immunization. PU.1 and SpiB double-deficient B cells have a survival defect after engagement of CD40 or Toll-like receptors (TLR), despite paradoxically enhanced plasma cell differentiation. PMID: 29127283 PU.1 can bind directly to the most-proximal Ets motif, which is essential for the transcriptional function of the mouse OX40L promoter in dendritic cells. PMID: 27708417 PU.1 suppresses Sirt1 translation via transcriptional promotion of miR-34a/-29c. PMID: 29162670 The analysis points to a critical role for Hoxa9 and PU.1 in distal regulation of c-myb expression in murine myeloid cells during iL-6-induced cell differentiation. PMID: 27607579 Data suggest that site-specifically bound PU.1 dimers occupy an extended DNA interface downstream from 5prime-GGAA-3prime core consensus relative to its 1:1 counterpart, thus explaining apparent site size requirement for sequential dimerization of PU.1. PMID: 28790174 PU.1 levels affected the expression of mouse orthologs of many Alzheimer's diseas risk genes and the phagocytic activity of mouse microglial cells PMID: 28628103 These studies reveal an important role for PU.1 in the regulation of Igkappa transcription and rearrangement and a requirement for PU.1 and Spi-B in B cell development. PMID: 28062693 expression of an essential mediator of neutrophil terminal differentiation, the ets transcription factor PU.1, was significantly decreased in Hbb(th3/+) neutrophils in a model of beta-thalassemia PMID: 28325862 Moreover, the expression of a cell proliferation marker Ki67 was significantly decreased in tumors from the mice not taking doxycycline, compared with that of tumors from the mice continuously taking doxycycline. The present data strongly suggest that PU.1 functions as a tumor suppressor of myeloma cells in vivo. PMID: 28347818 the affinities of two sequence-divergent ETS homologs, PU.1 and Ets-1, to DNA sites harboring a hemi- and fully methylated CpG dinucleotide, were measured. PMID: 27270080 this study shows that the generation of central nervous system macrophages relies on the transcription factor PU.1 PMID: 27135602 this study shows that PU.1 functions as a positive regulator of CD11c gene expression by directly binding to the Itgax promoter and through transactivation of the Irf4 gene PMID: 28338898 Here we demonstrate that the transcription factors SPI1 (PU.1) and HOXC13 synergistically regulate Zfp521 expression, and identify the regions of the Zfp521 promoter required for this transcriptional activity. We also show that SPI1 and HOXC13 activate Zfp521 in a dose-dependent manner. PMID: 27506447 Authors report that PU.1 serves as a critical regulator of alternatively activated macrophage(AAM) polarization and promotes the pathological progress of asthmatic airway inflammation. PMID: 26101328 findings suggest that Gata1 & PU.1 transcription factors are only executing and reinforcing lineage choice once made. These results challenge the current prevailing model of early myeloid lineage choice PMID: 27411635 involved in osteoclast development by transactivating NFATc1 expression via direct binding to the NFATc1 promoter PMID: 26117255 GATA1 and PU.1 bind in vitro and in vivo the proximal promoter region of the RPS19 gene which is frequently mutated in Diamond-Blackfan Anemia. PMID: 26447946 PU.1 Suppresses Th2 Cytokine Expression via Silencing of GATA3 Transcription in Dendritic Cells PMID: 26361334 Taken together, our results suggest that the expression of NDRG2 potentially inhibits osteoclast differentiation and plays a role in modulating the signal transduction pathway responsible for osteoclastogenesis. PMID: 26546825 these data indicate an inhibitory role for PU.1 in the function of Tfh cells, germinal centers, and Tfh-dependent humoral immunity. PMID: 26363052 Our results suggest that complementary biological functions of PU.1 and Spi-B may be explained by their interaction with a similar set of regions in the genome of B cells. PMID: 25765478 PU.1 keeps macrophage-specific genes accessible during differentiation by preventing Polycomb repressive complex 2 binding to transcriptional regulatory elements. PMID: 26012552 Nfkb1 transcriptional activation by PU.1 and Spi-B promotes toll-like receptor-mediated B cell proliferation. PMID: 25733685 in addition to supporting early T-cell proliferation, PU.1 regulates the timing of activation of the core T-lineage developmental program. PMID: 25846797 These findings indicate that PU.1-mediated upregulation of CSF-1R is a critical effector of MLL leukemogenesis. PMID: 25529853 The Nogo-B-PirB axis controls macrophage-mediated vascular remodeling. PMID: 24278366 these results suggest that PU.1 and Spi-B activate Btk to oppose IL-7 responsiveness in developing B cells. PMID: 25505273 Runx-dependent PU.1 chromatin interaction and transcription of PU.1 are essential for both normal and leukemia stem cells. PMID: 25185713 miR-155 inhibits PU.1 expression, leading to Pax5 down-regulation and the initiation of the plasma cell differentiation pathway. PMID: 25288398 The transcription factors IRF8 and PU.1 negatively regulate plasma cell differentiation. PMID: 25288399 Deletion of p53 mice with a homozygous deletion of the upstream regulatory element in PU.1 results in more aggressive acute myeloid leukemia. PMID: 24121269 PU.1 overexpression resulted in upregulation of miR-191 and adipogenic inhibition. Likewise, PU.1 overexpression rescued the miR-191 decrease and resisted the adipogenic promotion caused by miR-191 oligonucleotide inhibitor. PMID: 25094047 spontaneous leukemias that develop in mice of the mixed 129S2/SvPas and C57BL/6 background of knockout mice arise by a pathway that does not involve biallelic PU.1 mutation. PMID: 25076114 our findings demonstrate that PU.1 contributes to the development of MLL leukemia, partially via crosstalk with the MEIS/HOX pathway. PMID: 24445817 Identification of a minimal set of DNA sequence and shape features that accurately predict both Pu.1 binding and nucleosome occupancy genome-wide. PMID: 24813947 Mice with PU.1 deficiency in T cells were protected from colitis, whereas treatment with antibody to IL-9 suppressed colitis PMID: 24908389 the expression control of Tal2 in hematopoietic cells PMID: 24086757 Data indicate that cultured Sfpi1(BN/BN) cells expressed elevated messenger RNA transcript and protein levels of E2F1, an important regulator of cell cycle entry. PMID: 24316397 Spi-1 inhibits mitochondrial apoptosis in vitro and in vivo through the transcriptional repression of Bim, a proapoptotic factor. PMID: 23852375 It was concluded that the conformational change in Runx1 induced by Pin1 represses PU.1 transcription in pre-monocytes and influences the commitment to the monocyte lineage. PMID: 24037986 PU.1 Expression Induces -50 kb Irf8 Enhancer Activity and Chromatin Remodeling. PMID: 23623495 PU.1 expression repressed genes with nearby adipocyte-specific PPARgamma binding sites, while a common macrophage-adipocyte gene expression program was retained. PMID: 23775123 these study analyzed PU.1 and cell cycle regulation in individual cells during early macrophage and B cell development. PMID: 23868921 Biosensor-surface plasmon resonance (SPR) reveals a striking kinetic profile for DNA binding by the PU.1 transcription factor domain. At low salt concentrations, it binds high-affinity cognate DNA with a very slow association rate constant. PMID: 23416556 Data indicate that FOS, SPI1, KLF10, TFEC, and PRDM16 show robust transcriptional cross-regulation and are often associated with osteoclastogenesis. PMID: 23340137 Data conclude that both GM-CSF and FLT3L act through PU.1 to activate the 5.3 Kb CD11c proximal promoter in DCs and to induce differentiation of monocyte-derived DCs. PMID: 23284905 A critical role for PU.1 initiates microRNA-142 expression and modulates interleukin (IL)-6 expression in response to Toll-like receptor (TLR)4 signaling. PMID: 23509362 Spi-1, Fli-1 and Fli-3 (miR-17-92) oncogenes contribute to a single oncogenic network controlling cell proliferation in friend erythroleukemia. PMID: 23056458 Maintenance of Gata3 protein levels by Myb and Notch signaling is linked to the ability to retain T-cell identity in response to PU.1. PMID: 23444353

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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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