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Merck

C1224

Caspase 3 human

≥85% (SDS-PAGE), recombinant, expressed in E. coli (C-terminal histidine-tagged), buffered aqueous glycerol solution, ≥1.0 units/mg protein

Synonim(y):

Apopain, CPP32, Yama

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Wybierz wielkość

10 μG

2235,50 zł

2235,50 zł

Cena katalogowa2630,00 złZaoszczędź 15%

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Informacje o tej pozycji

UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
Specific activity:
≥1.0 units/mg protein
Assay:
≥85% (SDS-PAGE)
Recombinant:
expressed in E. coli (C-terminal histidine-tagged)

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recombinant

expressed in E. coli (C-terminal histidine-tagged)

assay

≥85% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

≥1.0 units/mg protein

mol wt

~30 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Quality Level

Gene Information

human ... CASP3(836)

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Ta pozycja
AB3623C9598C1099
specific activity

≥1.0 units/mg protein

specific activity

-

specific activity

-

specific activity

≥1,000 units/mg protein

Gene Information

human ... CASP3(836)

Gene Information

human ... CASP3(836)

Gene Information

human ... CASP3(836)

Gene Information

human ... CASP8(841)

assay

≥85% (SDS-PAGE)

assay

-

assay

-

assay

≥90% (SDS-PAGE)

form

buffered aqueous glycerol solution

form

-

form

buffered aqueous solution

form

buffered aqueous solution

recombinant

expressed in E. coli (C-terminal histidine-tagged)

recombinant

-

recombinant

-

recombinant

expressed in E. coli (C-terminal histidine tagged)

mol wt

~30 kDa

mol wt

-

mol wt

antigen 32 kDa

mol wt

~30 kDa

General description

Research area: Apoptosis

Human recombinant C-terminal histidine tagged caspase 3 is a fully active protein consisting of 17 kDa and 13.5 kDa subunits; the 13.5 kDa subunit contains the histidine tag.

Application

Caspase 3 human has been used to digest human r-vimentin. It has also been used in caspase-3 inhibition assay and protease inhibition assay.

This product may also be used in cell-based apoptosis assay.

Biochem/physiol Actions

Caspase 3 is a member of the CED-3 subfamily of caspases and is responsible for the cleavage of many key proteins such as the nuclear enzyme poly(ADP-ribose) polymerase (PARP), the inhibitor of caspase-activated deoxyribonuclease (ICAD), and gelsolin, a protein involved in apoptosis regulation. Caspase 3 is considered to be an effector caspase, activating pro-caspase 6 and pro-caspase 9 in vitro. Caspase 3 can be activated by caspase 8, caspase 6, and granzyme B.
Member of the CED-3 subfamily of caspases and responsible for the cleavage of many key proteins such as the nuclear enzyme poly(ADP-ribose) polymerase (PARP), the inhibitor of caspase-activated deoxyribonuclease (ICAD), and gelsolin, a protein involved in apoptosis regulation.

Physical form

Solution in 10% (w/v) glycerol containing 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM DTT, 1 mM EDTA, 0.1% CHAPS

Preparation Note

Caspase 3 is synthesized as a 32 kDa proenzyme. The active enzyme is a heterodimer of two large (17 kDa) subunits and two small (12 kDa) subunits.

Other Notes

One unit will cleave 1.0 μmole of N-acetyl-Asp-Glu-Val-Asp-pNA per min at pH 7.4 at 25 °C.
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Klasa składowania

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Discovery of indole tetrafluorophenoxymethylketone-based potent novel small molecule inhibitors of caspase-3
Samiulla DS, et al.
Organic and Medicinal Chemistry Letters, 2(1), 27-27 (2012)
Cross-presentation of caspase-cleaved apoptotic self antigens in HIV infection
Rawson PM, et al.
Nature Medicine, 13(12), 1431-1431 (2007)
A peptide-based positron emission tomography probe for in vivo detection of caspase activity in apoptotic cells
Hight MR, et al.
Clinical Cancer Research, 20(8), 2126-2135 (2014)
Regulation of spermatogenic cell apoptosis by the pro-apoptotic proteins in the testicular tissues of mammalian and avian species
Zakariah M, et al.
Animal Reproduction Science (2022)
Petra Procházková et al.
PloS one, 9(10), e109900-e109900 (2014-10-04)
Iron homeostasis in cells is regulated by iron regulatory proteins (IRPs) that exist in different organisms. IRPs are cytosolic proteins that bind to iron-responsive elements (IREs) of the 5'- or 3'-untranslated regions (UTR) of mRNAs that encode many proteins involved

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