Anti-Histone is an indirect solid phase enzyme immunoassay (ELISA) for measurement of IgG class autoantibodies to histone in human serum or plasma.
Contents of Kit
Package size 96 determinations 1. Qty.1 Divisible microplate consisting of 12 modules of 8 wells each, coated with highly purified histones (H1, H2A, H2B, H3 and H4). Ready to use. 2. 6 vials, 1.5 ml each Anti-Histone Calibrators (A-F) in a serum/buffer matrix (PBS, BSA, NaN3 <0.1% (w/w)) containing: IgG: 0; 12.5; 25; 50; 100; and 200 U/ml. Ready to use. 3. 2 vials, 1.5 ml each Anti-Histone Controls in a serum/buffer matrix (PBS, BSA, NaN3 <0.1% (w/w)) positive and negative , for the respective concentrations see the enclosed QC insert. Ready to use. 4. 1 vial, 20 ml Sample buffer (Tris, NaN3 <0.1% (w/w)), yellow, concentrate (5×). 5. 1 vial, 15 ml Enzyme conjugate solution (PBS, Proclin 300 <0.5% (v/v)), (light red) containing polyclonal rabbit anti-human IgG; labelled with horseradish peroxidase. Ready to use. 6. 1 vial, 15 ml TMB substrate solution. Ready to use. 7. 1 vial, 15 ml Stop solution (contains acid). Ready to use. 8. 1 vial, 20 ml Wash solution (PBS, NaN3 <0.1% (w/w)), concentrate (50×).
Storage
1. Store the kit at 2-8 °C. 2. Keep microplate wells sealed in a dry bag with desiccants. 3. The reagents are stable until expiration of the kit. 4. Do not expose test reagents to heat, sun or strong light during storage and usage. 5. Diluted sample buffer and wash buffer are stable for at least 30 days when stored at 2-8 °C.
Detection Range
0-200 U/ml.
Detection Limit
1 U/mL
Citations
Publication ()
Have you cited DEIA1683 in a publication? Let us know and earn a reward for your research.
Background
In eukaryotic cells, the nucleosome is the basic unit of chromatin and consists of 147 base pairs of DNA and histone octamers (including one H2A-H2B tetramer and two H3-H4 dimers). The N- and C- terminals of these histones can be post-translationally modified, such as acetylation, phosphorylation, methylation, and ubiquitination, and these post-transcriptional modifications can alter the electronic charge and structure of the histone tails that bind to the DNA, thereby altering the chromatin state and subsequent gene expression. To date, histone modifications have been found to play important roles in a variety of cellular processes.
Figure 1. Nucleosome structures (Source: Taylor EL, et al. 2021)
The amino acid sequences of histones are well conserved from archaea to humans. Addition of acetyl groups to the lysine residues of histones neutralizes the positive charge on the lysine residues, thereby weakening the interaction between histones and DNA. Thus, histone acetylation activates transcription. Histone methylation is a reversible reaction catalyzed by histone methyltransferases (HMT) and histone demethylases (HDM) that can occur at lysine or arginine residues of histones. Histone methylation plays an important role in transcriptional regulation, and depending on the methylated residues, histone methylation can be regarded as an active or repressive mark for transcription. Histone phosphorylation occurs on serine, threonine and tyrosine. A number of kinases and phosphatases regulate histone phosphorylation, which has been implicated in chromatin condensation, DNA damage response and transcription. Lysine residues of histones can be heavily modified by ubiquitin. Ubiquitinating enzymes (E1 activator, E2 ligase, and E3 ligase) and deubiquitinating enzymes regulate histone ubiquitination associated with genome stability, cell cycle, and transcription.
Dynamic changes in histone modifications as epigenetic marks modulate chromatin status and play an important role in neurogenesis and neurological diseases. Complex histone modifications such as acetylation and methylation are differentially associated with neuronal development and disease, and in some cases gene-specific changes in histone modifications regulate the expression of key genes associated with neurogenesis and neurological disease. Moreover, the spatiotemporal dynamics of histone modifications contribute to the complexity of neurogenesis and neurological diseases.
References
1. Taylor EL, et al. Histone Mutations and Bone Cancers. Adv Exp Med Biol. 2021;1283:53-62.
2. Park J, et al. The role of histone modifications: from neurodevelopment to neurodiseases. Signal Transduct Target Ther. 2022 Jul 6;7(1):217.
Creative Diagnostics products are for RESEARCH USE ONLY, please make sure your review is research based.
Required fields are marked with *
Terms and conditions:
We will select high-quality review customers and offer a $30 coupon for your next purchase.
All product reviews must be submitted in the English language.
Creative Diagnostics will not share any personal information of applicants, and all information will be treated with strict confidentiality and will not be sold or disclosed to a third party.
References
Sirtuins and their role as physiological modulators of metabolism
The sirtuins are a family of highly evolutionary conserved NAW-dependent deacetylases (SIRT1, 2, 3, 5). Certain human sirtuins (SIRT4, 6) have, in addition, an ADP-ribosyltransferase activity. SIRT1 and SIRT2 are located in the nucleus and cytoplasm; SIRT3 exists predominantly in mitochondria, and SIRT6 is located in the nucleus. The mammalian sirtuins have emerged as key metabolic sensors that directly link environmental nutrient signals to metabolic homeostasis. SIRT1 is involved in the regulation of gluconeogenesis and fatty acid oxidation, as well as inhibiting lipogenesis and inflammation in the liver. In addition, they contribute to the mobilization of fat in white adipose tissue, sense nutrient availability in the hypothalamus; regulate insulin secretion in the pancreas; as well as modulating the expression of genes responsible for the activity of the circadian clock in metabolic tissues. Sirtuins are implicated in a variety of cellular functions ranging from gene silencing, through the control of the cell cycle, to energy homeostasis. Caloric restriction, supported by polyphenols, including resveratrol, which is the SIRT1 activator, plays a special role in maintaining energy homeostasis. On a whole body level, the wide range of cellular activities of the sirtuins suggests that they could constitute a therapeutic target to combat obesity and related metabolic diseases. In addition, this work presents the current state of knowledge in the field of sirtuin activity in relation to nutritional status and lifespan.
Prognostic Relevance of HJURP Expression in Patients with Surgically Resected Colorectal Cancer
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Authors: Kang, Dong Hyun; Woo, Jongsoo; Kim, Hyeongjoo; Kim, Soo Youn; Ji, Sanghee; Jaygal, Gunn; Ahn, Tae Sung; Kim, Han Jo; Kwak, Hyoung Jong; Kim, Chang-Jin; Baek, Moo-Jun; Jeong, Dongjun
HJURP is a key factor for CENP-A deposition and maintenance in centromeres. The role of mis-regulation of histone chaperones in cancer initiation and progression has been studied. However, its role in colorectal cancer is still unclear. In this study, we aimed to evaluate the expression of HJURP in 162 colorectal cancer tissue. To investigate the function of HJURP in the colorectal cancer cell, we suppressed HJURP expression by siRNA and confirmed proliferation, migration, invasion, and anchorage independent of colony forming ability. The association between HJURP expression levels and clinicopathological factors was evaluated in 162 CRC tissues using immunohistochemistry. The overall survival rate in patients of HJURP high expression was higher than those in HJURP low expression in CRC. Suppressing HJURP expression decreased cellular proliferation, invasion, and migration in four CRC cell lines: HT29, HCT116, SW480, SW620 in vitro study. Our findings revealed that the knockdown of HJURP suppressed the proliferation, migration, invasion, and tumorigenicity in CRC cells. Due to its strong association with CRC, HJURP could be a potential prognostic biomarker and a novel target for drug discovery.