Recombinant Human Phd Finger Protein 6 (PHF6) Protein (His)

Name: Recombinant Human Phd Finger Protein 6 (PHF6) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06832P
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 Phd Finger Protein 6 (PHF6) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8IWS0
Target Symbol	PHF6
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMAYCRKHKKTAHNSEAADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMVCSFYICYATLHLICCFKFRVHPKFIQSSENLK
Expression Range	2-312aa
Protein Length	Full Length of Mature Protein
Mol. Weight	39.2 kDa
Research Area	Epigenetics And Nuclear Signaling
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 regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription.
Subcellular Location	Nucleus. Nucleus, nucleolus. Chromosome, centromere, kinetochore. Note=Nuclear, it particularly localizes to the nucleolus.
Database References	HGNC: 18145 OMIM: 300414 KEGG: hsa:84295 STRING: 9606.ENSP00000329097 UniGene: PMID: 28747286 PHF6 mutations occur at a low frequency in pediatric acute myeloid leukemia in both female and male patients PMID: 27885656 PHF6 defects most likely result in their loss of function and have a substantial effect on the evolution into the aggressive types of myeloid neoplasms, associated with other concomitant genetic defects including RUNX1 mutations PMID: 27479181 The mutations of the gene encoding plant homeodomain (PHD)-like finger protein 6 (PHF6) contribute to the pathogenesis of the X-linked intellectual disability disorder Borjeson-Forssman-Lehmann syndrome. PMID: 27633282 PHF6 localizes to the sub-nucleolar fibrillar center where it binds to rDNA-coding sequences. PHF6 mediates the overall levels of ribosome biogenesis within a cell. PMID: 27165002 Our results suggest that PHF6 may function as an oncogenic factor in several types of cancer. We also hypothesize that PHF6 may also play its role in a tissue-specific manner. Our findings suggest further investigations regarding the exact role of PHF6 in tumor types. PMID: 26561469 Female phenotypes of Borjeson-Forssman-Lehmann syndrome patients with PHF6 mutations PMID: 25099957 Our RBBP4-PHF6 complex structure provides insights into the molecular basis of PHF6-NuRD complex interaction and implicates a role for PHF6 in chromatin structure modulation and gene regulation. PMID: 25601084 Phf6 is a "lineage-specific" cancer gene that plays opposing roles in developmentally distinct hematopoietic malignancies. PMID: 25737277 The PHF6 tumor suppressor gene was targeted in acute lymphoblastic leukemia by microRNA-128-3p. PMID: 24895337 Our report confirms that PHF6 loss in females results in a recognizable phenotype overlapping with Coffin-Siris syndrome and distinct from Borjeson-Forssman-Lehmann syndrome. PMID: 24380767 Recurrent microdeletion was detected in Xq26.3, causing loss of PHF6 expression, a potential tumor suppressor gene, and the miR-424, which is involved in the development of acute myeloid leukemia. PMID: 24674452 The findings show that de novo mutations in PHF6 in females result in a recognisable phenotype which overlap with Borjeson-Forssman-Lehmann syndrome but also has additional distinct features, thus adding a new facet to this disorder. PMID: 24092917 these data support the hypothesis that PHF6 may function as a transcriptional repressor using its ePHD domains binding to the promoter region of its repressed gene PMID: 24554700 Data suggest that mutations of PHF6 are associated with chronic myeloid leukemia (CML) progression. PMID: 22928734 These results reveal that the key function of PHF6 is involved in regulating rRNA synthesis, which may contribute to its roles in cell cycle control, genomic maintenance, and tumor suppression. PMID: 23229552 PHF6 interacts with the nucleosome remodeling and deacetylation complex and is localized primarily in the nucleoplasm and nucleolus. PMID: 22720776 in T-cell acute lymphoblastic leukemia, PHF6 mutations are a recurrent genetic abnormality associated with mutations of NOTCH1, JAK1 and rearrangement of SET-NUP214. PMID: 21880637 Our data suggest that PHF6 mutation might play a role in tumorigenesis not only of T-cell acute lymphoblatic leukemia, but also acute myelogenous leukemia and hepatocellular carcinoma. PMID: 21736506 PHF6 as a tumor suppressor gene mutated in acute myeloid leukemias (AML) and extend the role of this X-linked tumor suppressor gene in the pathogenesis of hematologic tumors. PMID: 21030981 Borjeson-Forssman-Lehmann syndrome (BFLS) may represent a cancer predisposition syndrome and that mutations of PHF6 contribute to T-cell acute lymphoblastic leukemia. PMID: 20806366 these results identify PHF6 as a new X-linked tumor suppressor in T-ALL and point to a strong genetic interaction between PHF6 loss and aberrant expression of TLX transcription factors in the pathogenesis of this disease. PMID: 20228800 A novel, widely expressed zinc-finger (plant homeodomain[PHD]-like finger) gene had 8 different missense and truncation mutations in 7 familial and 2 sporadic cases of BFLS (p. 661). PMID: 12415272 ...mutations within a novel widely expressed zinc-finger gene (PHF6) have been described in nine families with Borjesson-Forssman-Lehmann syndrome... p. 1208 PMID: 14714741 The gene, PHF6, implicated in the Borjeson-Forssman-Lehmann syndrome has recently been identified. p. 1295 PMID: 14714754 A study of 9 families with PHF6 muations revealed that the phenotype is milder and more variable than previously described and evolves with age; seven missense mutations and two truncation mutations were identifed PMID: 14756673 By finding a PHF-6 mutation in a family with Borjeson-Forssman-Lehmann syndrome it was speculated that there is a mutational hot spot in the gene. PMID: 15241480 novel mutation results in exon skipping and mild Borjeson-Forssman-Lehmann syndrome PMID: 15466013 Success of PHF6 screening in males suspected of having Borjeson-Forssman-Lehmann syndrome is markedly increased if there is a positive family history and/or skewed X-inactivation is found in the mother. PMID: 15994862 we describe a novel mutation that changes a residue within the first plant homeodomain zinc finger motif of PHF6 in a family with classical features of Borjeson-Forssman-Lehmann syndrome PMID: 19264739

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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.