Recombinant Human Chromobox Protein Homolog 5 (CBX5) Protein (His&Myc)

Name: Recombinant Human Chromobox Protein Homolog 5 (CBX5) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04754P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Chromobox Protein Homolog 5 (CBX5) 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	P45973
Target Symbol	CBX5
Synonyms	Antigen p25; CBX5; CBX5_HUMAN; CG8409; Chromobox 5; Chromobox homolog 5 (HP1 alpha homolog; Drosophila); Chromobox homolog 5; Chromobox protein homolog 5; Epididymis luminal protein 25; HEL25; Heterochromatin protein 1 alpha; Heterochromatin protein 1; Heterochromatin protein 1 homolog alpha; HP1 alpha; HP1 alpha homolog; HP1; HP1A; HP1Hs alpha; Su(var)205
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MGKKTKRTADSSSSEDEEEYVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSESNKRKSNFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKETAKS
Expression Range	1-191aa
Protein Length	Full Length
Mol. Weight	29.7 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	Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins.
Subcellular Location	Nucleus. Chromosome. Chromosome, centromere.
Database References	HGNC: 1555 OMIM: 604478 KEGG: hsa:23468 STRING: 9606.ENSP00000209875 UniGene: PMID: 29467217 These data indicates that up-regulated HP1alpha, SUV39H1, and H3K9me3 in glioma cells are functionally associated with glioma pathogenesis and progression, and may serve as novel biomarkers for future diagnostic and therapeutic targeting of brain tumors. PMID: 28946550 Data suggest that SUMOylated heterochromatin protein 1-alpha (HP1alpha)alpha is a critical epigenetic-regulator of DNA-repair in breast cancer (BCa) that could define chemotherapy responsiveness. PMID: 27107417 findings suggest that heterochromatin-mediated gene silencing may occur in part through sequestration of compacted chromatin in phase-separated HP1 droplets, which are dissolved or formed by specific ligands on the basis of nuclear context PMID: 28636604 Data show that SALL4 promotes the expression of Glut1 and open chromatin through a HP1alpha-dependent mechanism. PMID: 28759035 These data suggests that up-regulated HP1A and H3K9me3 in glioma cells are functionally associated with glioma pathogenesis and progression. PMID: 28623138 Loss of HP1alpha and gamma isoforms inhibits the upregulation of Suv39h1 and H3K9me3 that is observed under stress conditions. PMID: 28059589 we showed the essential role of HP1 in regulating HR through BRCA1/BARD1-mediated accumulation of FANCJ and CtIP at DSB sites. This mechanism may affect tumorigenesis and chemosensitivity and is thus of high clinical significance. PMID: 27399284 the dynamic string-like behavior of HP1alpha's N-terminal tail underlies the enhancement in H3 binding due to phosphorylation. PMID: 26934956 We demonstrate that an hnRNPA1 and CBX5 bi-directional core promoter fragment does not comprise intrinsic capacity for specific CBX5 down-regulation in metastatic cells PMID: 26791953 HP1alpha plays an important role in the differentiation and angiogenic function of Endothelial Progenitor Cells. PMID: 25588582 Jra recruits the HP1a/KDM4A complex to its gene body region upon osmotic stress to reduce H3K36 methylation levels and disrupt H3K36 methylation-dependent histone deacetylation PMID: 25945750 HP1 regulates this gene's alternative splicing in a methylation-dependent manner by recruiting splicing factors to its methylated form. PMID: 25704815 PIP5K1A modulates ribosomal RNA gene silencing through its interaction with histone H3 lysine 9 trimethylation and heterochromatin protein HP1-alpha. PMID: 26157143 Paternal heterochromatin formation in human embryos is H3K9/HP1 directed and primed by sperm-derived histone modifications. PMID: 25519718 The results suggested that HP1 phosphorylation has an evolutionarily conserved role in HP1's recognition of H3K9me-marked nucleosomes. PMID: 25332400 Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that binds lysine 9-methylated histone H3 (H3K9me), a hallmark of heterochromatin, and plays a crucial role in forming higher-order chromatin structures. PMID: 24825911 CRL4B promotes tumorigenesis by coordinating with SUV39H1/HP1/DNMT3A in DNA methylation-based epigenetic silencing PMID: 24292684 RAD6 physically interacts with heterochromatin protein 1alpha and ubiquitinates HP1alpha at residue K154, thereby promoting heterochromatin protein 1alpha degradation through the autophagy pathway PMID: 25384975 These findings reveal a previously unrecognized but direct link between HP1 and CPC localization in the centromere and illustrate the critical role of borealin-HP1 interaction in orchestrating an accurate cell division. PMID: 24917673 Spatiotemporal dynamics of HP1A localization to centromere is governed by two distinct structural determinants. PMID: 25104354 The phosphorylation-dephosphorylation cycle of HP1alpha orchestrates accurate progression of cells through mitosis. PMID: 24786771 Binding of HP1alpha, HP1beta, and HP1gamma to the globular domain of histone H3 is differentially regulated by phosphorylation of residues H3T45 and H3S57. PMID: 24820035 CTCF may regulate vigilin behavior and thus indirectly influence the binding of HP1alpha to the satellite 2 locus. PMID: 24561205 these findings demonstrate that HP1(Hsalpha)-nucleosome interactions cause chromatin condensation, a process that regulates many chromosome events. PMID: 24415761 HP1alpha mutation W174A, which disrupts interactions with proteins containing the PxVxL motif did not affect interactions with the BZip protein. The HP1alpha W41A mutation, which prevents binding to methylated histones, exhibited greatly reduced FRET efficiency. PMID: 23392382 HP-1alpha/beta may be useful in the differential diagnosis of renal tumors, especially in the differentiation of chromophobe RCC and oncocytoma PMID: 23142018 We have identified CBX5 as a potential target regulating lung cancer survivals and the stem-like properties of lung CD133+- tumor stem-like cells (TSLCs). PMID: 22900142 The hinge region (HR) connecting the CD and C-terminal chromoshadow domain (CSD), and the CSD contributed to the selective binding of HP1alpha to histone H3 with trimethylated lysine 9 through weak DNA binding and by suppressing the DNA binding, respectively. PMID: 23142645 HP1-alpha and PADI4 are regulators of both immune genes and HERVs, and that multiple events of transcriptional reactivation in Multiple Sclerosis patients can be explained by the deficiency of a single mechanism of gene silencing. PMID: 23028349 Downregulation of the telomeric noncoding RNA requires SUV39H1 and HP1A. PMID: 22922742 These studies reveal a novel role for HP1 as a cofactor in tumor suppression, expand our mechanistic understanding of a KLF associated to human disease. PMID: 22318730 HP1 increases the chromatin association of VHL. PMID: 22234250 The finding that HP1 alpha is down-regulated primarily at the transcriptional level provides a new insight for the further elucidation of the detailed molecular mechanisms causing the HP1 alpha down-regulation in invasive breast cancer cells. PMID: 21374739 A link between mutant codanin-1 and the aberrant localization of HP1 alpha is supported by the finding that codanin-1 can be coimmunoprecipitated by anti-HP1 alpha antibodies erythroblasts from patients with congenital dyserythropoietic anemia type 1. PMID: 21364188 HP1alpha binding by INCENP or Shugoshin 1 (Sgo1) is dispensable for centromeric cohesion protection during mitosis of human cells, but might regulate yet unknown interphase functions of the chromosome passenger complex (CPC) or Sgo1 at the centromeres. PMID: 21346195 Recent findings and controversies concerning HP1 functions in mammalian cells in comparison to studies in other organisms, are reviewed. PMID: 20421743 ATRX185 is required for HP1a deposition in pericentric beta-heterochromatin of the X chromosome PMID: 20154359 The assembly of HP1 in the inner centromere and the localization of hMis14 at the kinetochore are mutually dependent in human chromosomes. PMID: 20231385 data suggest that HP1 chromoshadow-domains can benefit from the opening of nucleosomal structures to bind chromatin and that HP1 proteins use this property to detect and arrest unwanted chromatin remodeling PMID: 20011120 HP1alpha expression regulation is dependent on cell proliferation. PMID: 20049717 Heterochromatin protein 1 is extensively decorated with histone code-like post-translational modifications PMID: 19567367 reduction of YY1 expression in breast cancer cells could contribute to the acquisition of an invasive phenotype through increased cell migration as well as by reduced expression of HP1alpha PMID: 19566924 These results suggested that, although the majority of HP1alpha diffuses into the cytoplasm, some populations are retained in the centromeric region and involved in the association and segregation of sister kinetochores during mitosis. PMID: 11942629 identification of three amino acid residues I113, A114 and C133 in HP1alpha that are essential for the selective interaction of HP1alpha with BRG1 PMID: 12411497 developmentally regulated ARL5, with its distinctive nuclear/nucleolar localization and interaction with HP1alpha, may play a role(s) in nuclear dynamics and/or signaling cascades during embryonic development PMID: 12414990 histone H3 methylase Suv39h1 and the methyl lysine-binding protein HP1alpha directly interact with MBD of MBD1 in vitro and in cells PMID: 12711603 HP1 has a role in the recruitment but not in the stable association of Orc1p with heterochromatin PMID: 15454574 HP1alpha recruits endogenous HP1beta to the chromatin and this induces heterochromatin formation and enhanced histone lysine methylation. PMID: 15899859 Results describe the predominant nuclear localization of another Arp subfamily, Arp6, in vertebrate cells, and show its colocalization with heterochromatin protein 1 orthologs in pericentric heterochromatin. PMID: 16487625

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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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