Recombinant Human At-Rich Interactive Domain-Containing Protein 1A (ARID1A) Protein (His&Myc)

Name: Recombinant Human At-Rich Interactive Domain-Containing Protein 1A (ARID1A) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-02071P
Price: 349.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins, Recombinant proteins holiday sale

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Size

100ug

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Product Overview

Description	Recombinant Human At-Rich Interactive Domain-Containing Protein 1A (ARID1A) Protein (His&Myc) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O14497
Target Symbol	ARID1A
Synonyms	actin-dependent regulator of chromatin subfamily F member 1; ARI1A_HUMAN; ARID domain containing protein 1A; ARID domain-containing protein 1A; ARID1A; AT rich interactive domain 1A (SWI like); AT rich interactive domain 1A; AT rich interactive domain containing protein 1A; AT-rich interactive domain-containing protein 1A; B120; BAF250; BAF250A; BM029; brain protein 120 ; BRG1 associated factor 250; BRG1 associated factor 250a; BRG1-associated factor 250; BRG1-associated factor 250a; C1ORF4; chromatin remodeling factor p250 ; chromosome 1 open reading frame 4; ELD; hELD; hOSA1; matrix-associated; MRD14; Osa homolog 1; OSA1; OSA1 nuclear protein ; P270; SMARCF1; SWI like protein; SWI SNF complex protein p270; SWI-like protein; SWI/SNF complex protein p270; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily f, member 1; SWI/SNF-related
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	SLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCNKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMM
Expression Range	1976-2231aa
Protein Length	Partial
Mol. Weight	32.4 kDa
Research Area	Cancer
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	Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. 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 postmitotic 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 postmitotic 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.
Subcellular Location	Nucleus.
Database References	HGNC: 11110 OMIM: 603024 KEGG: hsa:8289 STRING: 9606.ENSP00000320485 UniGene: Hs.468972
Associated Diseases	Coffin-Siris syndrome 2 (CSS2)
Tissue Specificity	Highly expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, and PBL, and at a much lower level in heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas.

Gene Functions References

Cells lacking ARID1A show enhanced AURKA transcription, which leads to the persistent activation of CDC25C, a key protein for G2/M transition and mitotic entry. PMID: 30097580
the correlation between the loss of ARID1A immunoreactivity and reduced ARID1B levels indicates that ARID1B could be an attractive target for anti-cancer therapy. PMID: 29890703
these data suggest that the combined treatment with PI3K inhibitor BKM120 and PARP inhibitor olaparib may be a promising therapeutic regimen for the treatment of gastric cancer, and ARID1A deficiency could serve as a potential predictive therapeutic biomarker. PMID: 29767248
Although Genome-Wide Association studies have not been carried out in the field of alcohol-related hepatocellular carcinoma (HCC), common single nucleotide polymorphisms conferring a small increase in the risk of liver cancer risk have been identified. Specific patterns of gene mutations including CTNNB1, TERT, ARID1A and SMARCA2 exist in alcohol-related HCC. [review] PMID: 28296015
The authors find that ARID1A has a dominant role in maintaining chromatin accessibility at enhancers, while the contribution of ARID1B is evident only in the context of ARID1A mutation. PMID: 28967863
ARID1A and human epidermal growth factor receptor-2 (Her-2) status were found to be independent prognostic factors of both overall survival (OS) and disease free survival (DFS). PMID: 28543794
ARID1A expression loss was associated with poor overall survival in Asians with gastric cancer. [meta-analysis] PMID: 27354232
the significant correlation was achieved between the negative ARID1A expression and the FIGO stage of endometrium-related gynecological cancers, but not the other characteristics. PMID: 28466574
This metaanalysis indicated that Gastric Cancer or Colorectal Cancer with ARID1A alteration might be a marker of poor prognosis. The ARID1A alteration of Gastric Cancer may result from different epigenetic factors. PMID: 28937020
Low ARID1A expression is associated with clear cell and endometrioid carcinoma of the ovary and the endometrium. PMID: 29451900
Loss of PTEN and ARID1A expression is highly specific for malignancy in effusion pathology PMID: 29170871
We propose a signaling cascade involving ARID1A, GADD45B and DUSP1 as mediators of the romidepsin effects in GCC cells. PMID: 27572311
head and neck squamous cell carcinoma patients with tumors having high level of miR-31 expression and high levels of Nanog/OCT4/Sox2/EpCAM expression, together with low level of ARID1A expression, were found to have the worst survival PMID: 27528032
loss of ARID1A leads to accumulation of ROS; elesclomol may be used to target ARID1A-mutant gynecologic cancer cells PMID: 27486766
genomic data and clinical features of four patients carrying a small 1p36.11 microduplication encompassing the complete ARID1A gene PMID: 27906199
Data show that 38 samples of 82 ovarian clear cell carcinoma (CCC) specimens presented no BAF250a expression, and 50 samples exhibited the loss of at least one subunit of the SWI/SNF complex. PMID: 27340867
Partial loss (i.e. in one tissue section some cells stained positive for BAF250a while other cells, usually an adjacent group, were negative) of BAF250a protein was identified in 36% (9/25) of rectovaginal DIE samples, 40% (2/5) of endometriosis lesions involving the PSLN, 30% (6/20) of endometriomas, and also in 25% (5/20) of endometrium from controls. PMID: 26832958
In the very high-risk Bladder Cancer patients , several genes had a higher frequency of mutations than reported in the The Cancer Genome Atlas database, including ARID1A . Mutation associations with receipt of neoadjuvant chemotherapy, nodal involvement, metastatic disease development, and survival were analyzed. PMID: 27520487
Tumors accumulate ARID1A mutations. PMID: 27172896
ARID1A silencing could significantly enhance the capability of migration and invasion in lentivirus miR-144-3p cells. PMID: 29073615
we identified concurrent ARID1A and ARID1B inactivating mutations with consequent loss of protein expression in the undifferentiated component of approximately one-quarter of dedifferentiated endometrial and ovarian carcinomas PMID: 27562491
Our study provides a novel insight into the modulatory function and mechanism of ARID1A in PI3K/AKT signaling in gastric cancer PMID: 27323812
Of the 34 undifferentiated endometrial carcinomas examined, 17 (50%) exhibited SWI/SNF complex inactivation, with 11 tumors showing complete loss of both ARID1A and ARID1B, 5 showing complete loss of BRG1 and 1 showing complete loss of INI1. Ten of the remaining 17 undifferentiated carcinomas showed the following alterations: 5 tumors (15%) showed loss of ARID1A only with intact ARID1B, BRG1, and INI1 expression. PMID: 28863077
BAF250a loss in AE is consistently associated with the development of BAF250a-negative endometriosis-associated cancers and appears to be an early event in most of these cases. PMID: 27051059
Transcriptome analysis revealed ARID1A knockdown led to miR-503 upregulation. CDKN2A was identified as a target of miR-503, which contributes to cell senescence. Thus, the data suggests that ARID1A deficiency promote KRAS(G12D)-driven pancreatic tumorigenesis through miR-503/CDKN2A-mediated senescence. PMID: 28942143
ARID1A may be a primary driver of carcinogenesis in a subset of esophageal adenocarcinomas PMID: 28440661
ARID1A mutation inactivates the apoptosis-promoting function of p53 by upregulating HDAC6, indicating that pharmacological inhibition of HDAC6 is a therapeutic strategy for ARID1A-mutated cancers. PMID: 28737768
ARID1A mutation can be an early stage event in the oncogenic transformation of endometriosis cells giving rise to ovarian clear cell carcinoma. PMID: 28483516
ARID1A expression is significantly decreased in higher stages of urothelial carcinoma and its aggressive variants. PMID: 27137986
Our data suggests that deficiency or loss of functional mutations of ARID1A in HCC cells might contribute to the increased activity of certain cancer-promoting lncRNAs. PMID: 28716731
ARID1A loss lacks prognostic significance in early stage colorectal adenocarcinoma. PMID: 26980037
ARID1A may play an important role in the early events of gastric carcinogenesis. PMID: 28031120
loss of ARID1A is more common in advanced GC and is related to EBV positivity and MMR deficiency PMID: 26067140
ARID1A protein and mRNA expression was lower in intrahepatic cholangiocarcinoma tissue than in normal liver tissue. PMID: 27433094
Most HCCs had an increased level of ARID1A mRNA. PMID: 26589513
loss of ARID1A protein expression found in TU-OC-2 cells. PMID: 26960408
Inactivating mutations in ARID1A may be involved in a novel pathway of carcinogenesis in biliary carcinomas PMID: 27334809
loss of ARID1A shortened time to cancer-specific mortality, and to recurrence of cancer when adjusting for potential confounders (Meta-Analysis) PMID: 26384299
loss of ARID1A protein expression caused by inactivating mutations reactivates TERT transcriptional activity and confers a survival advantage of tumor cells by maintaining their telomeres. PMID: 26953344
All cases with ARID1A expression are overlapped with H2B high expression. Among 15 cases with ARID1A and H2B coexpression, 13 are invasive ductal carcinoma and 2 are mucinous carcinoma. Our results indicate that ARID1A gene may be involved in carcinogenesis of some subtypes of breast cancer. PMID: 26904685
The action of ARID1A in carcinogenesis differs between adenofibroma-related clear cell carcinoma and endometriosis-related clear cell carcinoma. PMID: 25913291
we focus on the relationships of ARID1A mutations with ovarian and endometrial cancers[review] PMID: 26572704
analysis of ARID1A, CDH1, cMET and PIK3CA expression and related microRNA expression in gastric cancer PMID: 26334097
The loss of ARID1A was correlated with late-stage and endometriosis-associated ovarian clear cell carcinoma. ARID1A expression may predict the risk of recurrence. PMID: 26945423
Complete or partial loss of ARID1A expression is considered an independent poor prognostic factor in patients with gastric cancer. PMID: 26826411
ARID1A positively regulates Klf15 expression with PGR to inhibit epithelial proliferation at peri-implantation. Our results suggest that Arid1a has a critical role in modulating epithelial proliferation which is a critical requisite for fertility PMID: 26378916
Our results indicate that the Arid1a tumour suppressor gene has a key role in regulating ovarian endometrioid carcinoma differentiation PMID: 26279473
Arid1A role in genome-wide transcriptional regulation by SWI/SNF complexes. PMID: 26716708
Identification of this undescribed functional NLS within ARID1A contributes vital insights to rationalize the impact of ARID1A missense mutations observed in patient tumors. PMID: 26614907
Data showed that ARID1A interacts with ATR via its C-terminal region, which mediates its recruitment to DNA double-strand breaks. PMID: 26069190

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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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