Product Details

Uniprot No.

Target Names

BANF1

Alternative Names

Barrier-to-autointegration factor (Breakpoint cluster region protein 1) [Cleaved into: Barrier-to-autointegration factor, N-terminally processed], BANF1, BAF BCRG1

Species Reactivity

Human

Immunogen

A synthesized peptide from human BANF1 protein

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

1H11

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, IHC, FC

Recommended Dilution

Application	Recommended Dilution
IHC	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Immunohistochemistry (IHC) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

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.

Description

Barrier-to-autointegration factor 1 (BANF1) is a highly conserved DNA-binding protein that plays essential roles in nuclear envelope assembly, chromatin organization, and mitotic progression. This small but functionally critical protein anchors chromatin to the inner nuclear membrane and participates in post-mitotic nuclear reformation, making it a key subject of investigation in cell cycle research, nuclear architecture studies, and investigations into premature aging syndromes such as Néstor-Guillermo progeria syndrome, where BANF1 mutations have been identified.

This recombinant rabbit monoclonal antibody, clone 1H11, offers researchers the reproducibility and consistency that comes with sequence-defined production. Unlike traditional hybridoma-derived antibodies, recombinant technology ensures that every lot performs identically, eliminating the variability that can compromise longitudinal studies or multi-site collaborations. The antibody was raised against a synthetic peptide derived from human BANF1 and has been affinity-purified for optimal specificity.

Validation studies demonstrate reliable performance across multiple experimental platforms. Immunohistochemistry testing in paraffin-embedded human tissues, including colorectal cancer and testis samples, shows clear nuclear staining patterns consistent with BANF1's known localization, with effective results at 1:100 dilution using citrate buffer antigen retrieval. Flow cytometry analysis in MCF-7 breast cancer cells confirms intracellular detection capability, showing distinct positive signal separation from isotype controls when cells are properly fixed and permeabilized.

Whether you are investigating nuclear envelope dynamics, exploring BANF1's role in cancer biology, or studying chromatin organization during cell division, this antibody provides a dependable tool validated for immunohistochemistry and flow cytometry applications in human samples.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Target Background

Function

Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging.; (Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.; (Microbial infection) In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication.

Gene References into Functions

BAF and BAF-L might contribute to the shaping of the spermatozoon nucleus and, after fertilisation, its transition to the male pronucleus. PMID: 28684548
we demonstrate that BAF is necessary to modulate prelamin A effects on chromatin structure PMID: 26701887
Findings support the value of using BioID to identify unrecognized constituents of distinct subcellular compartments refractory to biochemical isolation and reveal VRK2A as a transmembrane kinase in the NE that regulates BAF. PMID: 28637768
It has been concluded that the LEM domain, responsible for binding to the chromatin protein BAF, undergoes a conformational change during self-assembly of emerin N-terminal region. PMID: 27960036
antiviral capabilities of the barrier to autointegration factor (BAF/BANF1) and how its function and regulation places BAF at the junction of multiple pathways protecting a cell's genetic integrity PMID: 26842478
The findings unveil a unique mechanism where the nuclear periphery proteins lamin-A/C, LAP2alpha and BAF1 are assembled into a protein complex during mitosis in order to regulate assembly and positioning of the mitotic spindle. PMID: 26092935
results demonstrate a novel function of BAF as an epigenetic regulator of HSV lytic infection; hypothesize that BAF facilitates Herpes Simplex Virus IE and E gene expression by recruiting the SETD1A methyltransferase to viral IE and E gene promoters PMID: 26015494
Vaccinia virus B1 kinase is needed for multiple critical junctures in the poxviral life cycle in a manner that is both dependent on and independent of BAF. PMID: 26223647
BAF is a cytosolic DNA sensor that leads to exogenous DNA avoiding autophagy. PMID: 25991860
These data suggest that VRK3-mediated phosphorylation of BAF may facilitate DNA replication or gene expression by facilitating the dissociation of nuclear envelope proteins and chromatin during interphase. PMID: 25899223
Association of emerin with nuclear BAF in cells required the LEM domain (residues 1-47). PMID: 25052089
The BANF1, alanine 12 threonine (A12T) mutant is impaired in its ability to bind DNA while its interaction with nuclear envelope proteins is unperturbed. PMID: 25495845
Altogether, these data demonstrate that phosphoregulation of BAF by viral and cellular enzymes modulates this protein at multiple molecular levels, thus determining its effectiveness as an antiviral factor and likely other functions as well. PMID: 24600006
Data indicate that the major phosphatase responsible for dephosphorylation of of BAF Ser-4 to be protein phosphatase 4 catalytic subunit. PMID: 24265311
Activation of BANF1 possibly suppresses S100A9 expression and inactivates c-Jun, resulting in suppression of cutaneous inflammation PMID: 23664529
Emerin and BAF associated only in histone- and lamin-B-containing fractions. The S173D mutation specifically and selectively reduced GFP-emerin association with BAF by 58% PMID: 24014020
The decrease in vaccinia virus transcription caused by loss of B1 kinase can be rescued by depletion of BAF. PMID: 23891157
The accumulation of wild-type prelamin A detected in restrictive dermopathy as well as the accumulation of mutated forms identified in familial partial lipodystrophy and mandibuloacral dysplasia affect the nuclear localization of BAF protein. PMID: 22935701
BAF associated in vivo with SET/I2PP2A (protein phosphatase 2A inhibitor; blocks H3 dephosphorylation) and G9a (H3-K9 methyltransferase), but showed no detectable association with HDAC1 or HATs. PMID: 22127260
A single copy of normal BANF1 is sufficient to avoid the development of Nestor-Guillermo progeria syndrome. PMID: 21932319
The absence of direct binding of BAF to MAN1-C eliminates disruption of this interaction as the cause of the premature aging phenotype. PMID: 21966431
Data determined that the knockdown of Banf1 alters the cell cycle distribution of both human and mouse ESCs by causing an uncharacteristic increase in the proportion of cells in the G2-M phase of the cell cycle. PMID: 21750191
The authors demonstrate that the DNA binding and dimerization capabilities of BAF are essential for its function as an antipoxviral effector, while the presence of emerin is not required. PMID: 21880762
These nuclear abnormalities are rescued by ectopic expression of wild-type BANF1, providing evidence for the causal role of this mutation. PMID: 21549337
Cooperation of ATP-dependent remodeling, histone methylation, and kinase activation, followed by H1 displacement, is a prerequisite for the subsequent displacement of histone H2A/H2B catalyzed by PCAF and BAF. PMID: 21447625
These findings are supported by coimmunoprecipitation of prelamin A or progerin with BAF in vivo and suggest that BAF could mediate prelamin A-induced chromatin effects. PMID: 20581439
BAF and emerin have dynamic roles in genome integrity and might help couple DNA damage responses to the nuclear lamina network PMID: 19759913
The barrier-to-autointegration factor (BAF)-binding domain of emerin is located at the emerin N-terminus (residues 70-178) and includes the LEM-domain. PMID: 11792821
BAF is required for the assembly of emerin and A-type lamins at the reforming nuclear envelope during telophase and may mediate their stability in the subsequent interphase. PMID: 11792822
BAF may have a role in regulating emerin-GCL repressor complexes PMID: 12493765
report that BAF protein is a component of preintegration complexes isolated from HIV-1-infected cells PMID: 12663813
HB and barrier-to-autointegration factor are the same protein PMID: 14523012
BAF protein was detected in activated but not resting CD4+ T-lymphocytes. BAF bound directly to both p55 Gag and its cleaved product, matrix. PMID: 14645565
Data describe the mobility of barrier-to-autointegration factor to its partners emerin, LAP2 beta, and MAN1 in the nuclear membrane of living HeLa cells. PMID: 15109603
LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly PMID: 15546916
BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation. PMID: 16155580
phosphorylation at Ser175 regulates the dissociation of emerin from BAF PMID: 16204256
Ser-4 phosphorylation inhibits BAF binding to emerin and lamin A, and thereby weakens emerin-lamin interactions during both mitosis and interphase. PMID: 16371512
These results indicate that barrier-to-autointegration factor is required for the integrity of the nuclear lamina and normal progression of S phase in human cells. PMID: 17519288
We now show that BAF acts as a potent inhibitor of poxvirus replication unless its DNA-binding activity is blocked by B1-mediated phosphorylation. PMID: 18005698
analyses in human cells showed that barrier-to-autointegration factor (BAF), assembled first at the distinct ;core' region of the telophase chromosome and formed an immobile complex by binding with NE proteins, such as lamin A and emerin. PMID: 18628300

Hide All

Involvement in disease

Nestor-Guillermo progeria syndrome (NGPS)

Subcellular Location

[Barrier-to-autointegration factor]: Nucleus. Cytoplasm. Chromosome. Nucleus envelope.

Protein Families

BAF family

Tissue Specificity

Widely expressed. Expressed in colon, brain, heart, kidney, liver, lung, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen and testis. Not detected in thymus and peripheral blood leukocytes.

Database Links

HGNC: 17397

OMIM: 603811

KEGG: hsa:8815

STRING: 9606.ENSP00000310275

UniGene: Hs.433759

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Code	CSB-RA098504A0HU
Size	US$210
	Order now
Image	IHC image of CSB-RA098504A0HU diluted at 1:100 and staining in paraffin-embedded human colorectal 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 Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. IHC image of CSB-RA098504A0HU diluted at 1:100 and staining in paraffin-embedded human testis tissue 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 Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. Overlay Peak curve showing MCF-7 cells stained with CSB-RA098504A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/110⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/110⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.
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BANF1 Recombinant Monoclonal Antibody

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