Recombinant Human Myeloid Leukemia Factor 1 (MLF1) Protein (GST)

Name: Recombinant Human Myeloid Leukemia Factor 1 (MLF1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09209P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Myeloid Leukemia Factor 1 (MLF1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P58340
Target Symbol	MLF1
Synonyms	Hls7; MLF1; MLF1_HUMAN; Myelodysplasia myeloid leukemia factor 1; Myelodysplasia-myeloid leukemia factor 1; Myeloid leukemia factor 1; myeloid leukemia factor 1 variant 1; myeloid leukemia factor 1 variant 2; myeloid leukemia factor 1 variant 3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MFRMLNSSFEDDPFFSESILAHRENMRQMIRSFSEPFGRDLLSISDGRGRAHNRRGHNDGEDSLTHTDVSSFQTMDQMVSNMRNYMQKLERNFGQLSVDPNGHSFCSSSVMTYSKIGDEPPKVFQASTQTRRAPGGIKETRKAMRDSDSGLEKMAIGHHIHDRAHVIKKSKNKKTGDEEVNQEFINMNESDAHAFDEEWQSEVLKYKPGRHNLGNTRMRSVGHENPGSRELKRREKPQQSPAIEHGRRSNVLGDKLHIKGSSVKSNKK
Expression Range	1-268aa
Protein Length	Full Length
Mol. Weight	57.6kDa
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	Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus.
Subcellular Location	Cytoplasm. Nucleus. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body.
Protein Families	MLF family
Database References	HGNC: 7125 OMIM: 601402 KEGG: hsa:4291 UniGene: Hs.85195
Associated Diseases	A chromosomal aberration involving MLF1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with NPM1/NPM.
Tissue Specificity	Most abundant in testis, ovary, skeletal muscle, heart, kidney and colon. Low expression in spleen, thymus and peripheral blood leukocytes.

Gene Functions References

Mutation in HTT causes Huntington's disease (HD); aggregates of mutated HTT cause apoptosis in neurons of HD patients. Data suggest that both MLF1 and MLF2 preferentially interact with mutated N-terminal HTT; MLF1/MLF2 reduce number of neurons (Neuro2A cell line) containing mutant HTT aggregates and subsequent apoptosis. (HTT = Huntingtin protein; MLF = myeloid leukemia factor) PMID: 27840155
The data indicate that MLF1 serves as a proapoptotic antagonist that interacts with the HAX1/HtrA2-OMI/PARL (HOP) mitochondrial complex to modulate cell survival. PMID: 28137643
These findings suggest that MLF and the associated co-chaperones play a direct role in modulating gene transcription. PMID: 27984043
SNP associated with neuroblastoma resides upstream of the MLF1. Gene silencing of MLF1 in neuroblastoma cells results in significant growth inhibition. PMID: 28545128
Data indicte that acute myeloid leukemia (AML) with NPM1-MLF1 and AML with NPM1 mutations showed similar immunophenotypical and molecular features, including gene mutation patterns and gene expression profiling (GEP). PMID: 23403313
The subcellular localization of full-length human MLF1 is 14-3-3epsilon-independent. PMID: 23271436
changes in the subcellular localization of NPM, due to alterations in the relative abundance of NPM and NPM-MLF1 proteins, may contribute to the enhanced myeloid progenitor activity of Npm +/- cells PMID: 22193965
Data present the high-resolution crystal structure of this binding motif [MLF1(29-42)pSer34] in complex with 14-3-3epsilon and analyse the interaction with isothermal titration calorimetry. PMID: 22151054
MLF1 gene rearrangement is associated with acute myeloid leukemia. PMID: 20471513
phosphorylation of 14-3-3 binding site by MADM PMID: 12176995
These findings suggest that an NPM/MLF1 fusion is the primary molecular abnormality in t(3;5) MDS and AML with multilineage dysplasia, and that cases with NPM/MLF1 may be clinically distinct from other MDS-associated disease PMID: 14506644
Over-expression of MLF1 has little impact on skeletal muscle function in mice; progressive formation of protein aggregates in muscle are not necessarily pathogenic; MLF1 and MRJ may function together to ameliorate the toxic effects of mutant proteins. PMID: 17854834
shuttling of MLF1 is critical for the regulation of cell proliferation and a disturbance in the shuttling balance increases the cell's susceptibility to oncogenic transformation PMID: 17967869

FAQs

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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.