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Merck
CN

MABE443

Anti-BPTF Antibody, clone 15B1.1

clone 15B1.1, from mouse

别名:

Protein Bptf, BPTF

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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702

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产品名称

Anti-BPTF Antibody, clone 15B1.1, clone 15B1.1, from mouse

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

15B1.1, monoclonal

species reactivity

rat, mouse, human

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

isotype

IgG2bκ

NCBI accession no.

NP_789820

UniProt accession no.

E9Q6A7

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

100

Gene Information

human ... BPTF(2186)
mouse ... Bptf(207165)
rat ... Bptf(303617)

Physical form

Protein G Purified
Format: Purified
Purified mouse monoclonal IgG2bκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Analysis Note

Evaluated by Western Blotting in HeLa cell lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected BPTF in 10 µg of HeLa cell lysate.

Application

Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected BPTF in human testis, rat colon, and mouse colon tissue.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Nuclear Receptors
This Anti-BPTF Antibody, clone 15B1.1 is validated for use in Western Blotting and Immunohistochemistry (Paraffin) for the detection of BPTF .

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.

General description

Nucleosome-remodeling factor (NURF) subunit BPTF (UniProt E9Q6A7 & A2A654; also known as Bromodomain and PHD finger-containing transcription factor, Fetal Alzheimer antigen) is encoded by the Bptf (also known as 9430093H17Rik, Falz) gene (Gene ID 207165) in murine species. ATP-dependent chromatin remodeling complexes are classified into four major subfamilies (SWI/SNF, ISWI, CHD, and INO80). NURF is the founding member of ISWI remodeling complexes. Mammalian NURF is composed of BPTF, the ATPase SNF2L, and the Trp-Asp (WD) repeat protein pRBAP46/48, with BPTF being the largest subunit among the three. BPTF PHD finger-mediated binding of H3K4me3 stabilizes the NURF complex on chromatin, resulting in NURF-catalyzed nucleosome sliding. The NURF remodeling complex is essential for mammalian development and executes epigenetic regulation in multiple signaling pathways, including heat shock, TGF-beta/SMAD, JAK/STAT, WNT/beta-catenin, RB, and nuclear hormone receptors.
~322 kDa observed. Uncharacterized band(s) may appear in some lysates.

Immunogen

GST-tagged recombinant protein corresponding to mouse BPTF.

Other Notes

Concentration: Please refer to lot specific datasheet.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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相关内容

White Paper: Further considerations of antibody validation and usage.
Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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