RARA Recombinant Monoclonal Antibody

Code CSB-RA019338A0HU
Size US$210
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  • IHC image of CSB-RA019338A0HU diluted at 1:155 and staining in paraffin-embedded human breast cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

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Product Details

Uniprot No.
Target Names
Alternative Names
NR1B1 antibody; Nuclear mitotic apparatus protein retinoic acid receptor alpha fusion protein antibody; Nuclear receptor subfamily 1 group B member 1 antibody; Nucleophosmin retinoic acid receptor alpha fusion protein NPM RAR long form antibody; RAR alpha antibody; RAR antibody; RAR-alpha antibody; rara antibody; RARA_HUMAN antibody; RARalpha antibody; RARalpha1 antibody; Retinoic acid nuclear receptor alpha variant 1 antibody; Retinoic acid nuclear receptor alpha variant 2 antibody; Retinoic acid receptor alpha antibody; Retinoic acid receptor alpha polypeptide antibody
Species Reactivity
A synthesized peptide derived from human RARA
Immunogen Species
Homo sapiens (Human)
Rabbit IgG
Clone No.
Purification Method
It differs from different batches. Please contact us to confirm it.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Tested Applications
Recommended Dilution
Application Recommended Dilution
IHC 1:50-1:200
Troubleshooting and FAQs
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

The production of the RARA recombinant monoclonal antibody involves the utilization of DNA recombinant technology and in vitro genetic manipulation. Initially, an animal is immunized with a synthesized peptide derived from human RARA, enabling the isolation of B cells. The subsequent step involves screening and selecting positive B cells, followed by the identification of a single clone. PCR amplification of the light and heavy chains of the RARA antibody is carried out, and the resulting genes are inserted into a plasmid vector. This recombinant vector is then introduced into a host cell line to facilitate the expression of the antibody. The RARA recombinant monoclonal antibody is purified from the cell culture supernatant using affinity chromatography. This antibody exhibits a specific binding affinity for human RARA protein and can be effectively employed in ELISA and IHC applications.

The RARA protein binds to RA, which causes a conformational change of RARA, causing the dissociation of the corepressor complex and the recruitment of a coactivator complex, leading to the activation of transcription of target genes. RARA is involved in various biological processes, including embryonic development, differentiation, and homeostasis in adult tissues. It plays a critical role in the development of several tissues, including the central nervous system, the heart, and the hematopoietic system. RARA also participates in the pathogenesis of certain cancers, including acute promyelocytic leukemia (APL), where it is fused to a partner protein resulting in aberrant activation of its transcriptional activity.

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Target Background

Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. Formation of a complex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression. Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function. Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells. In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response.
Gene References into Functions
  1. Semiquantitative and quantitative analyses of the markers RARA and CRABP2 indicate their potential as biomarkers for tumor progression and their participation in nephroblastoma tumorigenesis PMID: 29378601
  2. The level of RARalpha gene expression as a potential prognostic factor in the pathogenesis of multiple myeloma. PMID: 29119395
  3. The data demonstrate that RARalpha drives integrin beta7-dependent adhesion and CCR9-mediated chemotaxis in CTCL cells. PMID: 28370539
  4. Silencing of PML-RAR and RARalpha2 results in similar increases in the constitutive expression of several granulocytic differentiation markers. PMID: 27419624
  5. RARA drives cyclin-dependent kinase expression, G1-S transition, and cell growth in T-cell lymphoma. PMID: 28412739
  6. Demonstrate that RARalpha was frequently elevated in gastric carcinoma and exerted oncogenic properties via positive feedback loop of IL-1beta/Akt/RARalpha/Akt signaling. PMID: 28035062
  7. Our findings unveil a novel essential oncogenic activity of PML/RARA in Acute promyelocitic leukemia PMID: 27626703
  8. Findings reveal a previously unrecognized role of c-Myc as a potential ceRNA for PML/RARalpha in acute promyelocytic leukemia. PMID: 27486764
  9. RARalpha regulates Arp2/3-mediated actin cytoskeletal dynamics through a non-genomic signaling pathway PMID: 26848712
  10. It has been shown that the AP-1 family member JunB and retinoic acid receptor alpha (RARa) mediate catalase transcriptional activation and repression, respectively, by controlling chromatin remodeling through a histone deacetylases-dependent mechanism. PMID: 27591797
  11. Work identifies the TP53 tumor suppressor as a novel target through which NPM1-RARA impacts leukemogenesis. PMID: 26754533
  12. Dual small interfering RNA (siRNA) silencing of RARalpha and RARgamma reversed RA blockade of P4-induced CK5. Using promoter deletion analysis, we identified a region 1.1 kb upstream of the CK5 transcriptional start site that is necessary for P4 activation and contains a putative progesterone response element (PRE PMID: 28692043
  13. High RARA expression is associated with acute myeloid leukemia. PMID: 28416638
  14. Data suggest that the binding of Z-10 to RXRalpha inhibited the interaction of RXRalpha with PML-RARalpha, leading to Z-10's selective induction of PML-RARalpha degradation. PMID: 28129653
  15. PML-RARa bcr1 fusion is not responsible for colorectal tumor development. PMID: 22167334
  16. overexpression of NLS-RARalpha promoted the proliferation of APL cells and inhibited their differentiation via the PI3K/AKT signaling pathway. PMID: 27840989
  17. r study demonstrated that ATRA cound promote differentiation while inhibit proliferation of acute promyelocytic leukemia NB4 cells via activating p38a protein after recruiting p38a-combinded NLS-RARa, while NLS-RARa could inhibit the effects of ATRA in the process. PMID: 27499693
  18. Low expression of RARalpha was independently associated with worse progression-free survival following platinum-based chemotherapy of advanced Non-small cell lung cancer. PMID: 27306217
  19. The classical counterpart of RARalpha, retinoid X receptor alpha (RXRalpha), was down-regulated in both cytoplasm and nucleus of A549 cells upon atRA addition. PMID: 26818829
  20. RAI1 polymorphisms rs4925102 and rs9907986 are predicted to disrupt the binding of retinoic acid RXR-RAR receptors and the transcription factor DEAF1, respectively, in Smith-Magenis and Potocki-Lupski syndromes patients. PMID: 26743651
  21. Data suggest that hematopoietically expressed homeobox protein (HHEX) downmodulation by promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein (PML-RARalpha) is a key event during acute promyelocytic leukemia (APL) pathogenesis. PMID: 27052408
  22. ATRA dramatically down regulated RARalpha protein levels and led to more DNA damage and ultimately resulted in the synergism of these two agents PMID: 26728137
  23. NPM-RAR binding to TRADD selectively inhibits caspase activation, while allowing activation of NFkappaB and JNK PMID: 25791120
  24. Suggest a novel role of PCGF2 in arsenic trioxide-mediated degradation of PML-RARA that PCGF2 might act as a negative regulator of UBE2I via direct interaction. PMID: 27030546
  25. down-regulation of the level of RAR alpha leads to increased expression of VDR in acute myeloid leukemia. PMID: 26969398
  26. Methylated arsenic metabolites bind to PML protein but do not induce cellular differentiation and PML-RARalpha protein degradation in acute promyelocytic leukemia. PMID: 26213848
  27. Novel insight into the functional difference of acquired mutations of PML-RARA both in vitro and in the clinical setting. PMID: 26537301
  28. our findings challenge the predominant model in the field and we propose that PML/RARA initiates leukemia by subtly shifting cell fate decisions within the promyelocyte compartment. PMID: 26088929
  29. RARalpha might be involved in the pathogenesis of varicocele as its expression is reduced in pathologic samples. PMID: 24992177
  30. The PML-region mutations were associated with response to Arsenic trioxide-based therapy (P < 0.0001), number of relapses (P = 0.001), and early relapse (P = 0.013)in acute promyelocytic leukemia patients. PMID: 26294332
  31. Data show that the tumor suppressor RASSF1A is a direct target of the PML/RARalpha-regulated microRNAs miR-181a/b cluster. PMID: 26041820
  32. These results suggest that overexpression of RARA enhances malignant transformation during mammary tumorigenesis. PMID: 25300573
  33. E2F1 is found to downregulate retinoic acid receptor alpha (RARalpha), a key factor determines the effectiveness of all-trans retinoic acid. PMID: 24608861
  34. bortezomib impairs the UPS that controls normal protein homeostasis by causing excessive accumulation of PML-RARA augmenting ER stress and leading to acute promyelocytic leukemia cell death PMID: 26026090
  35. CDKN2D repression by PML/RARalpha disrupts both cell proliferation and differentiation in the pathogenesis of acute promyelocytic leukemia. PMID: 25275592
  36. These results indicate that NPM-RAR, not RAR-NPM, is the prime mediator of myeloid differentiation arrest in t(5;17) APL. PMID: 23927396
  37. This study identifies a novel mechanism through which NPM-RAR affects leukemogenesis PMID: 25033841
  38. Data indicate that retinoic acid receptor (RAR) is crucial for regulating sodium taurocholate cotransporting polypeptide (NTCP) expression that determines permissiveness to hepatitis B virus (HBV) infection. PMID: 25550158
  39. Human miR-138 promotes tau phosphorylation by directly targeting the RARA and the associated GSK-3beta pathway. PMID: 25680531
  40. Down-regulation of NLS-RARalpha expression inhibited the proliferation and induced the differentiation of HL-60 cells. On the contrary, over-expression of NLS-RARa promoted proliferation and reduced the ATRA-induced differentiation of HL-60 cells. PMID: 24516348
  41. PML-RARalpha cooperates with HIF-1alpha to activate a pro-leukemogenic program. PMID: 24711541
  42. Results show that UTX interacts with the retinoic acid receptor alpha (RARalpha) and this interaction is essential for proper differentiation of leukemic U937 cells in response to retinoic acid. PMID: 25071154
  43. SUMO-1 modification of RARA is a potent mechanism for balancing proliferation and differentiation by controlling the stability of RARA in cancer cells. PMID: 24819975
  44. The current status of knowledge indicates that there might be inter- or overlapping actions between PPARg and RARs, and there might be an association of PPARg/RARs(RARa, RARb, and RARg) with renal diseases PMID: 24050824
  45. PML/RARalpha suppresses PU.1-dependent activation of the proteasome immunosubunits in acute promyelocytic leukemia. PMID: 23770850
  46. The presence of a mutation in the arsenic-binding domain of PML-RARA led to arsenic resistance in patients with acute promyelocytic leukemia. PMID: 24806185
  47. The objective was to describe the frequency of molecular subtypes of PML/RARalpha in patients with acute promyelocytic leukemia (APL) and their distribution according to risk of recurrence and cytomorphology PMID: 23612809
  48. provide evidence for the existence of a functional ternary complex containing TDG, CBP and activated RARalpha PMID: 24394593
  49. Differences in RAR and RXR subtype mRNA expression patterns in various PTCs may contribute to the immunochemistry data available, and may thus find exploitation in clinical oncology, particularly in the differential diagnosis of thyroid neoplasms. PMID: 23969901
  50. The tumor suppressor gene DAPK2 is induced by the myeloid transcription factors PU.1 and C/EBPalpha during granulocytic differentiation but repressed by PML-RARalpha in APL. PMID: 24038216

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Involvement in disease
Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation.
Subcellular Location
Nucleus. Cytoplasm.
Protein Families
Nuclear hormone receptor family, NR1 subfamily
Tissue Specificity
Expressed in monocytes.
Database Links

HGNC: 9864

OMIM: 180240

KEGG: hsa:5914

STRING: 9606.ENSP00000254066

UniGene: Hs.654583

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