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Merck

A4355

Sigma-Aldrich

Monoclonal Anti-ASPP1 antibody produced in mouse

~2 mg/mL, clone LXO54.2, purified immunoglobulin, buffered aqueous solution

Synonym(e):

Anti-Apoptosis-stimulating protein of p53, 1, Anti-PPP1R13B, Anti-protein phosphatase 1 regulatory subunit 13B

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

LXO54.2, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~175 kDa

Speziesreaktivität

mouse, human

Konzentration

~2 mg/mL

Methode(n)

immunoprecipitation (IP): suitable
microarray: suitable
western blot: 1-2 μg/mL using total cell extract of human osteogenic sarcoma, U-2-OS

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

Allgemeine Beschreibung

ASPP1 interacts with p53 to enhance p53-induced apoptosis.
Monoclonal Anti-ASPP1 (mouse IgG1 isotype) is derived from the hybridoma LXO54.2 produced by the fusion of mouse myeloma cells (SP2/0 cells) and splenocytes from BALB/c mice immunized with a recombinant fragment of human ASPP1, amino acids. Apoptosis-stimulating protein of p53, 1 (ASPP1) belongs to the ASPP family of proteins. This protein contains a proline-rich region, four ankyrin repeats, and an SH3 domain in the C-terminal end.

Immunogen

recombinant fragment of human ASPP1 (amino acids 1-308).

Anwendung

Monoclonal Anti-ASPP1 antibody can be used for western blot at 1-2 μg/mL using total cell extract of human osteogenic sarcoma, U-2-OS. The antibody can also be used for microarray and immunoprecipitation assays.

Biochem./physiol. Wirkung

Apoptosis-stimulating protein of p53, 1 (ASPP1) is known to stimulate RAS signalling which subsequently enhances p53-dependent apoptosis in cancer cells. Furthermore, ASPP1 can also induce p53-independent apoptosis by enhancing the apoptotic functions of p63 and p73. Monoclonal Anti-ASPP1 antibody recognizes human and mouse ASPP1.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Haftungsausschluss

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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WGK

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Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Xingwen Wang et al.
International journal of cancer, 141(7), 1422-1433 (2017-06-29)
Inactivation of p53 has been shown to correlate with drug resistance in tumors. However, in clear cell renal cell carcinoma (ccRCC), p53 is rarely mutated, yet the tumors remain highly insensitive to the conventional chemotherapeutic drugs. The underlying mechanisms responsible
Marcus M Schittenhelm et al.
Cell death & disease, 15(1), 25-25 (2024-01-10)
ASPP1 (PPP1R13B) belongs to a family of p53-binding proteins and enhances apoptosis by stimulation of p53-transactivation of selected proapoptotic target genes. It is preferentially expressed in hematopoietic stem cells (HSC) and together with p53 preserves the genomic integrity of the
Y Wang et al.
Cell death and differentiation, 20(4), 525-534 (2013-02-09)
RAS mutations occur frequently in human cancer and activated RAS signalling contributes to tumour development and progression. Apart from its oncogenic effects on cell growth, active RAS has tumour-suppressive functions via its ability to induce cellular senescence and apoptosis. RAS
ASPP proteins specifically stimulate the apoptotic function of p53
Samuels-Lev Y, et al.
Molecular Cell, 8(4), 781-794 (2001)
ASPP1 and ASPP2 are new transcriptional targets of E2F
Fogal V, et al.
Cell Death and Differentiation, 12(4), 369-369 (2005)

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