Recombinant Human Histone Acetyltransferase Myst2 (KAT7) Protein (GST)

Name: Recombinant Human Histone Acetyltransferase Myst2 (KAT7) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08455P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) KAT7.

Collections: High-quality recombinant proteins, Other recombinant proteins

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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Histone Acetyltransferase Myst2 (KAT7) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O95251
Target Symbol	KAT7
Synonyms	Hbo 1; HBO1; HBOa; Histone acetyltransferase binding to hORC1; Histone acetyltransferase binding to ORC1; Histone acetyltransferase KAT7; Histone acetyltransferase MYST2; K(lysine) acetyltransferase 7; KAT 7; KAT7; Lysine acetyltransferase 7; MOZ; MOZ YBF2/SAS3 SAS2 and TIP60 protein; MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2; MYST 2; MYST histone acetyltransferase 2; MYST protein 2; MYST-2; MYST2; MYST2_HUMAN; SAS 2; SAS2 and TIP60 protein 2; TIP60 protein 2; YBF2/SAS3; ZC2HC7
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHN
Expression Range	1-214aa
Protein Length	Partial
Mol. Weight	50.8kDa
Research Area	Transcription
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	Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryonic development. Some complexes also catalyze acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively), regulating DNA replication initiation, regulating DNA replication initiation. Specificity of the HBO1 complexes is determined by the scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4. H3K14ac promotes transcriptional elongation by facilitating the processivity of RNA polymerase II. Acts as a key regulator of hematopoiesis by forming a complex with BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and promoting erythroid differentiation. H3K14ac is also required for T-cell development. KAT7/HBO1-mediated acetylation facilitates two consecutive steps, licensing and activation, in DNA replication initiation: H3K14ac facilitates the activation of replication origins, and histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, promoting DNA replication licensing. Acts as a positive regulator of centromeric CENPA assembly: recruited to centromeres and mediates histone acetylation, thereby preventing centromere inactivation mediated by SUV39H1, possibly by increasing histone turnover/exchange. Involved in nucleotide excision repair: phosphorylation by ATR in response to ultraviolet irradiation promotes its localization to DNA damage sites, where it mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites. Acts as an inhibitor of NF-kappa-B independently of its histone acetyltransferase activity.; Plays a central role in the maintenance of leukemia stem cells in acute myeloid leukemia (AML). Acts by mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby facilitating the processivity of RNA polymerase II to maintain the high expression of key genes, such as HOXA9 and HOXA10 that help to sustain the functional properties of leukemia stem cells.
Subcellular Location	Nucleus. Chromosome. Chromosome, centromere. Cytoplasm, cytosol.
Protein Families	MYST (SAS/MOZ) family
Database References	HGNC: 17016 OMIM: 609880 KEGG: hsa:11143 STRING: 9606.ENSP00000259021 UniGene: PMID: 28719581 Hbo1 is another ERalpha coactivator that ubiquitinates ERalpha PMID: 28769019 Histone acetyltransferase binding to ORC1 (HBO1) is upregulated in bladder cancer. PMID: 28796367 The results demonstrate some connections between KAT7 upregulated in RA SFs and RA progression and present the inhibition of KAT7 activity as a novel therapeutic target for interfering RA disease. PMID: 28552525 Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2 have been presented. PMID: 28334966 KAT7-containing acetyltransferases associating with the Mis18 complex provides competence for histone turnover/exchange activity on alphoid DNA and prevents Suv39h1-mediated heterochromatin invasion into centromeres. PMID: 27270040 the possible binding sites and biological functions of HBO1, were identified. PMID: 27247147 Data show that HTLV-1 basic leucine zipper (bZIP) factor (HBZ) represses p53 activity by direct inhibition of the histone acetyltransferase (HAT) activity of p300/CBP and the HAT activity of HBO1: [HBZ] PMID: 26625199 This study demonstrates that CRL4(DDB2) is a novel ubiquitin ligase of HBO1. PMID: 26572825 Taken together, MYST2 is a repressed growth suppressor in AML mediating reduced acetylation of histone 4 at residue 5 and is associated with inferior AML patient survival. PMID: 26072331 Myst2-mediated histone acetylation may be required for recruitment of Oct4 to the Nanog promoter PMID: 25743411 Increase in the number of cells with cytoplasmic JADE1S correlated with activation of tubular cell proliferation and inversely correlated with the number of cells with nuclear JADE1S, supporting role of HBO1-JADE1 shuttling during organ regeneration. PMID: 24739512 Hbo1 modulated transcription by estrogen receptor-alpha. Hbo1 contributes to degradation of ER-alpha by ubiquitination through lysine 48. PMID: 24125069 Phosphorylated Hbo1 expression is associated with breast cancer. PMID: 23955388 alternate choice of subunits associated with HBO1 can switch its specificity between H4 and H3 tails PMID: 24065767 Gemcitabine resistance is dependent on Plk1-mediated phosphorylation of Orc2 and Hbo1. PMID: 23188630 Modulation of Fbxw15 levels was able to differentially regulate histone H3K14 acetylation and cellular proliferation by altering HBO1 levels. PMID: 23319590 The protein domains required for the assembly and function of HBO1/ING complexes were shown. Multiple PHD finger domains in different subunits bound the histone H3 N-terminal tail with a specificity towards lysine 4 methylation. PMID: 22144582 JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone acetylase and blocks replication licensing in response to stress PMID: 21856198 HBO1 was an important downstream molecule of ERalpha. PMID: 21040551 HBO1 promote MCM loading in vivo involves the stimulation of large-scale chromatin decondensation to allow access to the underlying DNA substrate. PMID: 20980834 results show that ING4 is a bivalent reader of the chromatin H3K4me3 modification and suggest a mechanism for enhanced targeting of the HBO1 complex to specific chromatin sites PMID: 20053357 H4 acetylation at origins by HBO1 is critical for DNA replication licensing. PMID: 20129055 inhibition by Set/TAF-1beta inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing PMID: 11978794 ordered recruitmenet to thyroid hormone-responsive promoters in vivo PMID: 12034878 Hbo1 is a positive regulatory factor for prereplicative complex assembly. PMID: 16428461 histone acetyltransferase binding to ORC-1 might play an important physiological role in human progesterone receptor signaling PMID: 16645042 reveal a direct regulatory connection between p53-responsive stress signaling and Hbo1-dependent chromatin pathways PMID: 17954561 Hbo1 depletion results in decreased DNA replication and a failure of Mcm complex binding to chromatin, both of which can be partially rescued by the ectopic expression of WT Hbo1 but not Hbo1-S57A PMID: 18250300 Jade-1/1L are crucial co-factors for HBO1-mediated histone H4 acetylation PMID: 18684714 HBO1 associates with replication origins specifically during the G1 phase of the cell cycle in a manner that depends on the replication licensing factor Cdt1, but is independent of the Cdt1 repressor Geminin. PMID: 18832067 Overexpression of MYST2 is associated with breast cancer. PMID: 19372580 Immunohistochemistry for Hbo1 in 11 primary human tumor types revealed strong Hbo1 protein expression in carcinomas of the testis, ovary, breast, stomach/esophagus, and bladder. PMID: 19393168

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.