Recombinant Mouse Protein Pml (PML) Protein (His&Myc)

Name: Recombinant Mouse Protein Pml (PML) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01690P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Protein Pml (PML) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q60953
Target Symbol	PML
Synonyms	Protein PML
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	LRCPSCQAQAKCPKLLPCLHTLCSGCLEAPGLQCPICKAPGQADANGEALDNVFFESLQRRLAVFRQIVDAQAACTRCKGLADFWCFECEQLICSKCFEAHQWYLKHEARPLADLRDNSVSSFLDSTRKSNIFCSNTNHRNPALTDIYCRGCAKPLCCTCALLDRNHSHLHCDIGEEIQQWHEE
Expression Range	60-243aa
Protein Length	Partial
Mol. Weight	28.1 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	Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum. Regulates RB1 phosphorylation and activity. Acts as both a negative regulator of PPARGC1A acetylation and a potent activator of PPAR signaling and fatty acid oxidation. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates PER2 nuclear localization and circadian function. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. Required for normal development of the brain cortex during embryogenesis. Plays a role in granulopoiesis or monopoiesis of myeloid progenitor cells. May play a role regulating stem and progenitor cell fate in tissues as diverse as blood, brain and breast. Shows antiviral activity towards lymphocytic choriomeningitis virus (LCMV) and the vesicular stomatitis virus (VSV).
Subcellular Location	Nucleus. Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body. Nucleus, nucleolus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side.
Database References	KEGG: mmu:18854 STRING: 10090.ENSMUSP00000082816 UniGene: PMID: 29302031 PML protein organizes heterochromatin domains where it regulates histone H3.3 deposition by ATRX and DAXX. PMID: 28341773 data support a model in which activation of myogenic differentiation results in PML NB loss, chromatin reorganization and DAXX relocalization, and provides a paradigm for understanding the consequence of PML loss in other cellular contexts, such as during cancer development and progression PMID: 28358373 a regulatory role of ZNF451-1 in fine-tuning physiological PML levels PMID: 27343429 PML loss promotes tumor development, providing a growth advantage to tumor cells that use autophagy as a cell survival strategy during stress conditions. PMID: 27545895 The data demonstrate a dual role of PML in protection and recovery after brain injury. PMID: 27468695 This study designates PML protein and PML-NBs to be major cellular components involved in the control of Herpes simplex virus 1 (HSV-1) latency, probably during the entire life of an individual. PMID: 27618691 Study found that Promyelocytic leukemia protein (PML) is broadly expressed across the gray matter, with the highest levels in the cerebral and cerebellar cortices. PML bodies are broadly involved in activity-dependent nuclear phenomena in adult neurons PMID: 25956166 These findings suggest that the UBC9/PML/RNF4 axis plays a critical role as an important SUMO pathway in cardiac fibrosis. Modulating the protein levels of the pathway provides an attractive therapeutic target for the treatment of cardiac fibrosis and heart failure. PMID: 28143738 PML contributes to the intrinsic restriction of HIV-1 infections in a cell type-dependent manner. PMID: 26703718 both the PML-RARA-driven competitive transplantation advantage and development of acute promyelocytic leukemia (APL) required DNMT3A PMID: 26595813 PML IV enhances global SUMO-1 conjugation, particularly that of p53, resulting in p53 stabilization and activation. PMID: 26578773 our findings challenge the predominant model in the field and we propose that PML/RARA initiates leukemia by subtly shifting cell fate decisions within the promyelocyte compartment. PMID: 26088929 DNA-binding-defective PML/RARA mutants could not repress the transcription of retinoic acid regulated genes. PMID: 25119106 pRB can interact with PML specifically during senescence, suggesting that signaling events in senescence regulate assembly of PML and pRB to establish heterochromatin and create a permanent cell cycle arrest. PMID: 24351540 Data suggest that acute promyelocytic leukemia (APL) differentiation is a default program triggered by clearance of promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein PML/RARA-bound promoters. PMID: 25258343 Our results add PML/TRIM19 to the growing list of TRIM proteins implicated in both intrinsic and innate immunity. PMID: 24586174 Oxidized PML spherical meshes recruit UBC9 and enhances PML sumoylation. PMID: 24637324 ORF61 encoded the viral ribonucleotide reductase large subunit is a second PML-modifying protein. PMID: 24371073 Activation of a promyelocytic leukemia-tumor protein 53 axis underlies acute promyelocytic leukemia cure. PMID: 24412926 Promyelocytic leukemia protein is a cell-intrinsic factor to inhibit parvovirus DNA replication. PMID: 24198403 PML and CycG2 mutually influence each other's functions following ionizing radiation. PMID: 23656780 Loss of PML gene from male mutant p53 mice resulted in reduced survival, associated with a high prevalence of soft tissue sarcomas; suggesting that in males, cooperation between these pathways drove a more aggressive disease. PMID: 23656786 Data indicate a role of promyelocytic leukemia protein (PML) in the regulation of metabolism and energy balance. PMID: 23986437 PML-RARalpha co-operates with Sox4 in acute myeloid leukemia development in mice. PMID: 23144197 role of PML in regulating cell adhesion, morphology, proliferation and migration PMID: 23555679 PML deficiency facilitates genomic instability and promotes HBsAg-related hepatocarcinogenesis, which also involves androgen and lipid metabolism. PMID: 23620081 PML protein and p53 reciprocally positively regulated each other during CPT-induced DNA damage, both of which were dependent on presenilin. PMID: 23306558 PML knockout mice present impaired cognitive function and reduced anxiety-related behavior. PMID: 23279884 These data are consistent with a model in which murine gammaherpesvirus 68 ORF75c could mediate direct ubiquitination of PML resulting in its degradation by the proteasome. PMID: 23541081 Tumor suppressor promyelocytic leukemia protein selectively activates NLRP3 inflammasome. PMID: 23430110 a unique role for PML in mTOR and EGFR inhibitor resistance and provide a strong rationale for a combination therapeutic strategy to overcome it. PMID: 23440206 the tumor suppressor PML acts as an important barrier in liver carcinogenesis and HCV-dependent liver pathology PMID: 22984515 SUMO interacting motif is dispensable for PML SUMOylation and interaction with RNF4 but is required for efficient PML ubiquitination, recruitment of proteasome components within NBs and proteasome-dependent degradation of PML in response to AsO PMID: 23028697 PML protein interacts with Moloney murine leukemia virus integrase and reverse transcriptase during Moloney murine leukemia virus infection. PMID: 22685230 Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation. PMID: 22773875 A PML-PPAR-delta pathway for fatty acid oxidation regulates hematopoietic stem cell maintenance. PMID: 22902876 PML and TBX2 act in an autoregulatory loop to control the effective execution of the senescence program. PMID: 22002537 a model in which Pin1 promotes PML degradation in an ERK2-dependent manner. PMID: 22033920 a novel functional connection between PML and the homologous recombination-mediated repair machinery PMID: 21998700 PML may limit fat accumulation by suppressing the differentiation of preadipocytes into adipocytes. PMID: 21846906 Setdb1 performs dual, but inseparable, functions at PML-NBs to maintain the structural integrity of PML-NBs and to control PML-NB-associated genes transcriptionally PMID: 21921037 Neither Daxx nor PML, the main players of ND10-based immunity, are required for the block to viral gene expression in the S/G2 phase. PMID: 21832009 study demonstrates a functional role for Pml in maintaining a specific open chromatin conformation of the Oct4 promoter region for its constant expression in stem cells PMID: 21360626 The authors find that combined inactivation of Pml and Tsc2 results in aberrant TORC1 activity both in pre-tumoural kidneys as well as in kidney lesions. PMID: 21387562 a key component for the differentiation of myeloid progenitor cells to macrophages PMID: 21427174 PML functions as a positive regulator of IFNgamma signaling PMID: 21115099 show that AXIN interacts with PML in vivo, and further that AXIN, PML and p53 form a ternary complex PMID: 21057547 PML is induced by interferon, leading to a marked increase of expression of PML isoforms and the number of PML nuclear bodies [Review] PMID: 21198351 expression of PML isoform PMLIV or PMLIVa, which is missing exon 5, inhibited rabies viral mRNA and protein synthesis, leading to a reduction in viral replication PMID: 20702643

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.