Recombinant Human ARID1A Protein (1976-2231 aa), His-Myc-tagged
Cat.No. : | ARID1A-2751H |
Product Overview : | Recombinant Human ARID1A Protein (1976-2231 aa) is produced by Baculovirus expression system. This protein is fused with a 10xHis tag at the N-terminal and a Myc tag at the C-terminal. Research Area: Cancer. Protein Description: Partial. |
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Description : | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. |
Source : | Baculovirus |
Species : | Human |
Tag : | His-Myc |
Form : | Tris-based buffer,50% glycerol |
Molecular Mass : | 32.4 kDa |
Protein length : | 1976-2231 aa |
AA Sequence : | SLAKRCVCVSNTIRSLSFVPGNDFE MSKHPGLLLILGKLILLHHKHPERK QAPLTYEKEEEQDQGVSCNKVEWWW DCLEMLRENTLVTLANISGQLDLSP YPESICLPVLDGLLHWAVCPSAEAQ DPFSTLGPNAVLSPQRLVLETLSKL SIQDNNVDLILATPPFSRLEKLYST MVRFLSDRKNPVCREMAVVLLANLA QGDSLAARAIAVQKGSIGNLLGFLE DSLAATQFQQSQASLLHMQNPPFEP TSVDMM |
Purity : | > 85% as determined by SDS-PAGE. |
Notes : | Repeated freezing and thawing is not recommended. Store working aliquots at 4 centigrade for up to one week. |
Storage : | The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 centigrade/-80 centigrade. The shelf life of lyophilized form is 12 months at -20 centigrade/-80 centigrade. |
Concentration : | A hardcopy of COA will be sent along with the products. Please refer to it for detailed information. |
Gene Name : | ARID1A AT rich interactive domain 1A (SWI-like) [ Homo sapiens ] |
Official Symbol : | ARID1A |
Synonyms : | ARID1A; B120; BAF250; BAF250a; C10rf4; P270; osa homolog 1; SWI-like protein; ELD; OSA1; hELD; BM029; hOSA1; C1orf4; SMARCF1; |
Gene ID : | 8289 |
mRNA Refseq : | NM_006015 |
Protein Refseq : | NP_006006 |
MIM : | 603024 |
UniProt ID : | O14497 |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (15)
Ask a questionThere are ongoing clinical trials investigating therapeutic strategies in ARID1A-altered cancers; however, direct targeting of ARID1A itself is challenging. These trials focus on exploiting vulnerabilities in ARID1A-deficient tumors or targeting related pathways. For example, trials are evaluating the use of PARP inhibitors, which exploit deficiencies in DNA repair pathways, in ARID1A-mutant ovarian and endometrial cancers. Other trials explore the combination of ARID1A-targeted therapies with immune checkpoint inhibitors or other targeted agents. These trials aim to improve outcomes for patients with ARID1A-altered cancers.
Yes, ARID1A is considered essential for normal development and survival. Studies in animal models have shown that loss of ARID1A function during embryonic development results in severe defects and embryonic lethality. In humans, germline mutations affecting both copies of the ARID1A gene lead to a developmental disorder known as Coffin-Siris syndrome. This highlights the critical role of ARID1A in normal development and its importance for survival.
Yes, mutations in ARID1A are frequently found in various types of cancer. ARID1A acts as a tumor suppressor and its inactivation or loss-of-function mutations have been implicated in several cancers, including ovarian, endometrial, gastric, and bladder cancers. These mutations can lead to dysregulated gene expression, altered chromatin remodeling, and disrupted cellular processes, fostering tumorigenesis.
ARID1A interacts with several proteins involved in chromatin remodeling and transcriptional regulation. Some of its known binding partners include SWI/SNF complex subunits (e.g., BRG1, BRM), transcription factors (e.g., p53, SNAI1, E2F1), and other chromatin-associated proteins (e.g., EZH2, HDAC1). These interactions contribute to the functional roles of ARID1A in modulating chromatin structure and gene expression.
ARID1A has primarily been studied in the context of cancer, where its mutations are frequently observed. However, emerging evidence suggests that ARID1A may also have implications in other diseases. Studies have implicated ARID1A in neurological disorders, such as intellectual disability and autism spectrum disorders, as well as in liver diseases like hepatocellular carcinoma and non-alcoholic fatty liver disease. Further research is needed to fully understand the role of ARID1A in these conditions.
Yes, ARID1A mutations can be inherited in some cases. Germline mutations in ARID1A have been identified in a small percentage of individuals with certain genetic syndromes, such as the Coffin-Siris syndrome. However, the majority of ARID1A mutations in cancer are somatic, meaning they occur spontaneously during the development of the tumor and are not inherited.
Targeting ARID1A directly is challenging due to its essential role in normal cellular processes. However, targeting downstream signaling pathways or molecules influenced by ARID1A alterations may hold therapeutic potential. For example, drugs targeting epigenetic modifiers, such as EZH2 inhibitors, have shown promise in ARID1A-mutated cancers. Additionally, exploring synthetic lethal interactions specific to ARID1A-deficient tumors may provide alternative therapeutic strategies in the future.
ARID1A mutations in cancer can have various consequences. Loss-of-function mutations or inactivation of ARID1A can lead to dysregulated gene expression and altered chromatin remodeling. This can affect cellular processes like DNA repair, cell cycle regulation, and cell differentiation, contributing to tumorigenesis and tumor progression. ARID1A mutations are often associated with aggressive tumor behavior and poor prognosis in certain cancer types.
ARID1A mutations are relatively common in certain types of cancer. They are most frequently observed in endometrial carcinoma, with mutations occurring in approximately 40% of cases. ARID1A mutations are also found in other gynecological cancers, such as ovarian and uterine clear cell carcinoma, with frequencies ranging from 20-60%. Additionally, ARID1A mutations are reported in various other cancer types, including gastric, colorectal, pancreatic, and renal cell carcinoma, albeit at lower frequencies. The prevalence of ARID1A mutations can vary depending on the specific cancer type and individual patient characteristics.
Currently, there are no drugs or compounds that directly target ARID1A. However, there are ongoing efforts to identify small molecules or inhibitors that can modulate ARID1A function or exploit vulnerabilities in ARID1A-deficient cancers. These approaches aim to indirectly target ARID1A by targeting related pathways or downstream effectors that are dependent on ARID1A activity.
Research on natural compounds or dietary factors specifically targeting ARID1A expression or activity is still limited. However, some studies have investigated the effects of certain compounds or dietary components on ARID1A-related pathways or functions. For example, curcumin, a compound found in turmeric, has been shown to affect ARID1A expression in certain cancers. Resveratrol, a compound found in grapes and red wine, has also been reported to modulate ARID1A expression and activity. However, more research is needed to fully understand the effects of natural compounds or dietary factors on ARID1A and their potential therapeutic implications.
Directly targeting ARID1A is difficult due to its essential role in normal cellular processes. However, ongoing research aims to develop therapeutic strategies targeting ARID1A-altered cancers indirectly. This includes exploring synthetic lethal interactions, combination therapies with drugs targeting related pathways or downstream effectors, and exploiting vulnerabilities in ARID1A-deficient tumors. It is an area of active investigation with the potential for future therapeutic advancements.
Yes, several post-translational modifications have been reported for ARID1A. These modifications can regulate its activity, stability, and subcellular localization. For example, phosphorylation of ARID1A by kinases like ATM and ATR can modulate its function in DNA damage response. Furthermore, acetylation, ubiquitination, and SUMOylation have also been observed to impact ARID1A activity.
Yes, ARID1A expression has been linked to certain prognostic and diagnostic markers in cancer. In ovarian cancer, loss of ARID1A expression has been associated with higher tumor stage, increased tumor invasiveness, and resistance to chemotherapy. Additionally, ARID1A expression levels have been suggested as a potential diagnostic marker for distinguishing between different subtypes of endometrial cancer.
Gene editing technologies like CRISPR/Cas9 have the potential to target specific genes, including ARID1A, for precise modifications. While it is theoretically possible to use CRISPR/Cas9 to target and modify ARID1A mutations, there are several challenges associated with this approach. First, efficiently delivering CRISPR/Cas9 components to the desired cells within a tumor can be technically challenging. Second, ARID1A mutations are often heterozygous, meaning they occur on one allele of the gene while the other allele remains normal. In such cases, selectively editing the mutated allele without affecting the normal allele can be difficult. Additionally, the potential off-target effects of CRISPR/Cas9 editing must be carefully assessed to avoid unintended consequences. Further research is needed to optimize gene editing strategies for targeting ARID1A mutations.
Customer Reviews (10)
Write a reviewWhether it is regarding experimental design, optimization of protocols, or troubleshooting issues, their expertise and prompt customer service help researchers overcome challenges efficiently.
With the manufacturer's unwavering dedication to delivering quality products and unparalleled technical support, I am confident in their ability to help me overcome any challenges and propel my research forward.
The ARID1A protein offered by the manufacturer is of exceptional quality and is expected to perfectly meet my experimental needs.
the ARID1A protein demonstrates significant relevance and potential in various trial applications, primarily focusing on inflammation, angiogenesis, and tissue remodeling.
Its purity and integrity are of the highest standard, ensuring reliable and reproducible results in my research.
The manufacturer's commitment to providing excellent technical support is commendable, as their dedicated team possesses the expertise to solve any issue or query that may arise during my experiments.
The manufacturer maintains stringent quality control measures to ensure the purity and stability of the protein, minimizing experimental variability and maximizing the accuracy of the data obtained.
Their prompt assistance and guidance contribute to enhancing the success and efficiency of my work with the ARID1A protein.
Another advantage of the ARID1A protein is its reliability and consistency, ensuring robust and reproducible results.
the manufacturer's support plays a crucial role in the successful implementation of trials involving the ARID1A protein.
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