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Key Documents

AB17003

Sigma-Aldrich

Anti-Bim Antibody, internal epitope, pan-Bim isoforms

Chemicon®, from rabbit

Sinónimos:

BOD

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About This Item

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

biological source

rabbit

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

mouse, human, rat

manufacturer/tradename

Chemicon®

technique(s)

western blot: suitable

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... TMBIM4(51643)

Specificity

Recognizes pan-Bim isoforms.

Immunogen

Epitope: internal epitope, pan-Bim isoforms
Synthetic peptide corresponding to amino acids 22-40 of human origin (O′Conneor et al. 1998). The sequence is identical to that of mouse and is different by one amino acid from that of rat.

Application

Research Category
Apoptosis & Cancer
Research Sub Category
BCL2 & Inhibition
This Anti-Bim Antibody, internal epitope, pan-Bim isoforms is validated for use in WB for the detection of Bim.
Western blot: 1:1000-1:2000

Human K562 cell lysate can be used as a positive control and a 23 kDa band can be detected.

Optimal working dilutions must be determined by end user.

Target description

23 kDa

Physical form

Format: Purified
ImmunoAffinity Purified
Immunoaffinity Purified immunoglobulin in 20 mM sodium phosphate, 250 mM NaCl, pH. 7.6, with 0.1% sodium azide as a preservative.

Storage and Stability

The undiluted antibody solution is stable for approximately 6 months when stored 2–8°C.

Analysis Note

Control
Skin/Skin Tumor

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Julia P Huang et al.
Oncology letters, 14(5), 5735-5742 (2017-11-09)
Enhancer of zeste homolog 2 (EZH2), a subunit of polycomb repressive complex 2, is a histone methyl-transferase and is considered to work cooperatively with histone deacetylases (HDACs) in the same protein complex to mediate gene transcription repression by increasing histone
NF-Y is essential for expression of the proapoptotic bim gene in sympathetic neurons.
Hughes, R; Kristiansen, M; Lassot, I; Desagher, S; Mantovani, R; Ham, J
Cell Death and Differentiation null
Shannon M Matulis et al.
Molecular cancer therapeutics, 8(5), 1197-1206 (2009-05-07)
Here, we report on the organic arsenical darinaparsin (ZIO-101, S-dimethylarsino-glutathione) and its anti-myeloma activity compared with inorganic arsenic trioxide. Darinaparsin induced apoptosis in multiple myeloma cell lines in a dose-dependent manner, and the addition of N-acetylcysteine, which increases intracellular glutathione
Abbas Hadji et al.
Oncotarget, 10(58), 6219-6233 (2019-11-07)
BCL-2 family proteins are central regulators of apoptosis and represent prime therapeutic targets for overcoming cell death resistance in malignancies. However, plasticity of anti-apoptotic members, such as MCL-1, often allows for a switch in cell death dependency patterns that lie
Sophie de Carné Trécesson et al.
Nature communications, 8(1), 1123-1123 (2017-10-27)
In tumours, accumulation of chemoresistant cells that express high levels of anti-apoptotic proteins such as BCL-XL is thought to result from the counter selection of sensitive, low expresser clones during progression and/or initial treatment. We herein show that BCL-XL expression

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