Recombinant Human AT-rich interactive domain-containing protein 3A (ARID3A)

Code CSB-YP858728HU
MSDS
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Source Yeast
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Code CSB-EP858728HU
MSDS
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Source E.coli
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Code CSB-EP858728HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP858728HU
MSDS
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Source Baculovirus
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Code CSB-MP858728HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ARID3A
Uniprot No.
Alternative Names
ARI3A_HUMAN; ARID domain containing 3A; ARID domain-containing protein 3A; ARID3A; AT rich interactive domain 3A (BRIGHT- like) protein; AT rich interactive domain 3A (BRIGHT-like); AT rich interactive domain-containing protein 3A; AT-rich interactive domain-containing protein 3A; B cell regulator of IgH transcription; B-cell regulator of IgH transcription; Bright; dead ringer like 1; dead ringer; Drosophila; homolog-like 1; Dead ringer-like protein 1; DRIL1; DRIL3; DRX; E2F binding protein 1; E2F-binding protein 1; E2FBP1; Homo sapiens AT rich interactive domain 3A (BRIGHT-like)
Species
Homo sapiens (Human)
Expression Region
1-593
Target Protein Sequence
MKLQAVMETL LQRQQRARQE LEARQQLPPD PPAAPPGRAR AAPDEDREPE SARMQRAQMA ALAAMRAAAA GLGHPASPGG SEDGPPGSEE EDAAREGTPG SPGRGREGPG EEHFEDMASD EDMKPKWEEE EMEEDLGEDE EEEEEDYEDE EEEEDEEGLG PPGPASLGTT ALFPRKAQPP QAFRGDGVPR VLGGQERPGP GPAHPGGAAH VAPQLQPPDH GDWTYEEQFK QLYELDGDPK RKEFLDDLFS FMQKRGTPVN RIPIMAKQVL DLFMLYVLVT EKGGLVEVIN KKLWREITKG LNLPTSITSA AFTLRTQYMK YLYPYECEKR GLSNPNELQA AIDSNRREGR RQSFGGSLFA YSPGGAHGML SSPKLPVSSL GLAASTNGSS ITPAPKIKKE EDSAIPITVP GRLPVSLAGH PVVAAQAAAV QAAAAQAAVA AQAAALEQLR EKLESAEPPE KKMALVADEQ QRLMQRALQQ NFLAMAAQLP MSIRINSQAS ESRQDSAVNL TGTNGSNSIS MSVEINGIMY TGVLFAQPPA PTPTSAPNKG GGGGGGSSSN AGGRGGNTGT SGGQAGPAGL STPSTSTSNN SLP
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation.
Gene References into Functions
  1. Data indicate ARID3a(+) B cells as a type of effector B cell, and link ARID3a expression in B lymphocytes to interferon alpha (IFNa)-associated inflammatory responses in systemic lupus erythematosus (SLE). PMID: 27522115
  2. results suggest that appropriate regulation of ARID3a is critical for normal development of both myeloid and B lineage pathways. PMID: 26685208
  3. These data reveal new functions for ARID3a in early hematopoiesis and suggest that knowledge regarding ARID3a levels in HSPCs could be informative for applications requiring transplantation of those cells. PMID: 25535283
  4. Systemic lupus erythematosus (SLE) patients had increased ARID3a+ B cells compared to healthy controls. ARID3a was not expressed in naive B cells of controls, but was abundant in SLE patients. Number of ARID3a+ B cells correlated with disease activity. PMID: 25185498
  5. miR-125b can act as an oncogene in B-cell acute lymphoblastic leukemia by targeting ARID3a and mediating its repression. PMID: 22469780
  6. These findings support the hypothesis that Epstein-Barr virus EBNA1 initiates transcription at the C promoter via interactions between multiple EBNA1 homodimers and cellular transcription such as E2F1, ARID3A and Oct-2. PMID: 22302879
  7. These results indicate both cooperative and interdependent roles for ARID3A and p53 in the transcriptional activation of p21(WAF1) in response to DNA damage. PMID: 22172947
  8. functions as a critical antagonist to the p16(INK4A)-Rb tumor suppressor machinery by regulating promyelocytic leukemia protein stability PMID: 22010578
  9. report that E2FBP1 inhibits accumulation of ICP0 RNA and, at the same time, is degraded via ICP0's herpes ubiquitin ligase 2 (HUL-2) activity upon HSV-1 infection. PMID: 21248039
  10. Bright/ARID3a inhibition causes increased developmental plasticity in mouse and human cells. PMID: 20680960
  11. Solution NMR structure of the ARID domain of human ARID3A. PMID: 20455271
  12. Results show that DRIL1 disrupts cellular protection against RAS(V12)-induced proliferation downstream of the p19(ARF)/p53 pathway. PMID: 11812999
  13. role in p53 regulatory pathway.(E2FBP1) PMID: 12136662
  14. Variations in Bright binding and matrix attachment region activity contribute to localized control of accessibility and therefore nonrandom gene use during V(D)J recombination. PMID: 12193717
  15. a putative p53-binding site was found, which specifically responded to p53, in the second intron of the E2FBP1/DRIL1 gene PMID: 12692263
  16. E2FBP1 modulates cell growth through down-regulation of promyelocytic leukemia bodies. PMID: 15017387
  17. Bright is not expressed in all human B lymphocyte subpopulations. PMID: 15203319
  18. TFII-I directly interacts with Bright through amino acids in Bright's protein interaction domain PMID: 16738337
  19. identify Bright as a contributor to accessibility of the IgH enhancer PMID: 17386101
  20. Id1 inhibited DNA binding by Dril1, and the two proteins co-localized in vitro and in vivo, providing a potential mechanism for suppression of fibrosis by Id1 through inhibition of the profibrotic function of Dril1. PMID: 18583319
  21. A palmitoylated pool of Bright is diverted to lipid rafts of resting B cells where it associates with signalosome components. PMID: 19214191

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Subcellular Location
Nucleus. Cytoplasm. Note=Shuttles between nucleus and cytoplasm.
Tissue Specificity
Widely expressed, with highest expression in skeletal muscle, thalamus, and colon.
Database Links

HGNC: 3031

OMIM: 603265

KEGG: hsa:1820

STRING: 9606.ENSP00000263620

UniGene: Hs.501296

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