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Merck
CN

MABE987

Anti-KSRP Antibody, clone Ab5

clone Ab5, from mouse

别名:

Far upstream element-binding protein 2, FUSE-binding protein 2, KH type-splicing regulatory protein, KSRP, p75, KSRP

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eCl@ss:
32160702
UNSPSC Code:
12352203

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产品名称

Anti-KSRP Antibody, clone Ab5, clone Ab5, from mouse

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

Ab5, monoclonal

species reactivity

human, mouse

technique(s)

immunocytochemistry: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

NP_003676

UniProt accession no.

Q92945

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... KHSRP(8570)

Analysis Note

Evaluated by Western Blotting in C2C12 mouse myoblast lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected KSRP in 10 µg of C2C12 mouse myoblast lysate.

Application

Anti-KSRP Antibody, clone Ab5, Cat. No. MABE987, is a highly specific mouse Monoclonal antibody, that targets KSRP and has been tested in Western Blotting and Immunocytochemistry.
Immunocytochemistry Analysis: A representative lot detected KSRP in HeLa and mouse neuroblastoma N1E-115 cells (Hall, M.P., et al. (2004). Mol Biol Cell. 15(2):774-786).
Western Blotting Analysis: 0.5 µg/mL from a representative lot detected KSRP in 10 µg of HeLa cell lysate.
Western Blotting Analysis: A representative lot detected KSRP in HeLa and mouse neuroblastoma N1E-115 cells (Hall, M.P., et al. (2004). Mol Biol Cell;15(2):774-86).
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Nuclear Receptors

Biochem/physiol Actions

Two KSRP immunoreactive bands are often observed using HeLa cell extracts, while a single band is seen using other cell extracts (e.g. C2C12 and N1E-115). The nature of the difference between the two bands is not yet known (PMID 14657238 & 9136930).

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

Far upstream element-binding protein 2 (UniProt Q92945; also known as FUSE-binding protein 2, KH type-splicing regulatory protein, KSRP, p75) is encoded by the KHSRP (also known as FBP2, FUBP2) gene (Gene ID 8570) in human. The KH-type splicing regulatory protein (KSRP) is an important regulator of several unstable mRNAs coding for pro-inflammatory mediators including TNF-α, IL-8, and iNOS. By binding to AU-rich elements (AREs) in the 3′-untranslated region (3′-UTR), KSRP recruits enzymes involved in the 5′- and 3′-mRNA decay. KSRP interacts with nucleic acids through four hnRNP KH domains and negatively regulates gene expression by promoting decay of target mRNAs. KSRP is also known to associate with Drosha and Dicer complexes and promote the maturation of microRNAs (miRNAs).
~80 kDa observed. Uncharacterized band(s) may appear in some lysates.

Immunogen

Recombinant protein corresponding to human KSRP.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

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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Jingxin Wang et al.
Proceedings of the National Academy of Sciences of the United States of America, 115(20), E4604-E4612 (2018-05-02)
RG-7916 is a first-in-class drug candidate for the treatment of spinal muscular atrophy (SMA) that functions by modulating pre-mRNA splicing of the SMN2 gene, resulting in a 2.5-fold increase in survival of motor neuron (SMN) protein level, a key protein

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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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