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Merck
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SAB1402978

Monoclonal Anti-MLL2 antibody produced in mouse

clone 2E1, purified immunoglobulin, buffered aqueous solution

Synonym(s):

AAD10, ALR, CAGL114, MLL4, TNRC21, Anti-AAD10, Anti-ALL1-related protein, Anti-ALR, Anti-CAGL114, Anti-Histone-lysine N-methyltransferase, Anti-KMS, Anti-KMT2B, Anti-KMT2D, Anti-Kabuki make-up syndrome, Anti-Kabuki mental retardation syndrome, Anti-MLL4, Anti-Myeloid/lymphoid or mixed-lineage leukemia 2, Anti-TNRC21

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About This Item

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
2E1, monoclonal
Application:
ELISA (i), WB
Citations:
4

Key Documents

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Quality Level

100

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

2E1, monoclonal

form

buffered aqueous solution

mol wt

antigen ~37.11 kDa

species reactivity

human

technique(s)

indirect ELISA: suitable, western blot: 1-5 μg/mL

isotype

IgG2aκ

NCBI accession no.

NM_003482

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MLL2(8085)

General description

Mixed-lineage leukemia 2 (MLL2), a histone methyltransferase that belongs to the trithorax group, is expressed ubiquitously in adult tissues. Structurally, MLL2 comprises plant homeodomain (PHD), Su(var)3-9, Enhancer-of-zeste and Trithorax (SET) domain, and a high mobility group (HMG) box. The MLL2 gene is mapped to human chromosome 12q13.12.

Immunogen

MLL2 (NP_003473.1, 1487 a.a. ~ 1586 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
SKLEGMFPAYLQEAFFGKELLDLSRKALFAVGVGRPSFGLGTPKAKGDGGSERKELPTSQKGDDGPDIADEESRGLEGKADTPGPEDGGVKASPVPSDPE

Biochem/physiol Actions

Mixed-lineage leukemia 2 (MLL2) regulates the expression of homeobox (Hox) genes. Mutations or haploinsufficiency in the MML2 gene is implicated in Kabuki syndrome, a multi-systemic disorder. It carries out methylation on the lysine 4 of histone H3 (H3K4). MLL2 plays a tumor suppressor role in Merkel cell carcinoma.

Physical form

Solution in phosphate buffered saline, pH 7.4

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

低风险生物材料
常规特殊物品
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Certificates of Analysis (COA)

Lot/Batch Number
11326-2E1
10278-2E1

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Reety Arora et al.
Viruses, 12(9) (2020-09-04)
Merkel cell carcinoma (MCC) is an uncommon, lethal cancer of the skin caused by either Merkel cell polyomavirus (MCPyV) or UV-linked mutations. MCPyV is found integrated into MCC tumor genomes, accompanied by truncation mutations that render the MCPyV large T
N Bögershausen et al.
Clinical genetics, 83(3), 212-214 (2012-11-08)
To unravel the system of epigenetic control of transcriptional regulation is a fascinating and important scientific pursuit. Surprisingly, recent successes in gene identification using high-throughput sequencing strategies showed that, despite their ubiquitous role in transcriptional control, dysfunction of chromatin-modifying enzymes
Alessandra Fasciani et al.
Nature genetics, 52(12), 1397-1411 (2020-11-11)
The genetic elements required to tune gene expression are partitioned in active and repressive nuclear condensates. Chromatin compartments include transcriptional clusters whose dynamic establishment and functioning depend on multivalent interactions occurring among transcription factors, cofactors and basal transcriptional machinery. However
Young-Wook Cho et al.
The Journal of biological chemistry, 282(28), 20395-20406 (2007-05-15)
PTIP, a protein with tandem BRCT domains, has been implicated in DNA damage response. However, its normal cellular functions remain unclear. Here we show that while ectopically expressed PTIP is capable of interacting with DNA damage response proteins including 53BP1

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