Skip to Content
MilliporeSigma

D7194

Sigma-Aldrich

DAPK3, active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

FLJ36473, ZIP

Slide 1 of 1
Sign Into View Organizational & Contract Pricing

Select a Size

10 μG
$433.00

$433.00


Check Cart for Availability

Request a Bulk Order

About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

Skip To


Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

product line

PRECISIO® Kinase

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

32-43 nmol/min·mg

mol wt

~79 kDa

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... DAPK3(1613)

Compare Similar Items

View Full Comparison

Show Differences

1 of 4

This Item
D7069SRP5018K4268
specific activity

32-43 nmol/min·mg

specific activity

42-57 nmol/min·mg

specific activity

115-156 nmol/min·mg

specific activity

578-782 nmol/min·mg

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

assay

≥70% (SDS-PAGE)

Gene Information

human ... DAPK3(1613)

Gene Information

human ... DAPK1(1612)

Gene Information

human ... DAPK2(23604)

Gene Information

human ... PRKD1(5587)

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in baculovirus infected Sf9 cells

recombinant

expressed in baculovirus infected Sf9 cells

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

form

buffered aqueous glycerol solution

mol wt

~79 kDa

mol wt

~71 kDa

mol wt

~67 kDa

mol wt

~131 kDa

Biochem/physiol Actions

DAPK3 or Death-associated protein kinase 3 (also known as ZIP) plays a role in apoptosis.DAPK3 is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. DAPK3 interacts with transcription and splicing factors as well as with pro-apoptotic protein Par-4 suggesting that it participates in multiple cellular processes. DAPK3 contains a leucine zipper structure at its C terminus and this region is responsible for binding to ATF4. The leucine zipper domain is necessary for the homodimerization of DAPK3 as well as for the activation of the kinase.

Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.

Legal Information

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Ute Preuss et al.
Nucleic acids research, 31(3), 878-885 (2003-02-01)
Death-associated protein (DAP)-like kinase (Dlk), also known as Zipper interacting protein (ZIP) kinase, is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. It interacts with transcription and splicing factors as well
Kasturi Markandran et al.
International journal of molecular sciences, 23(1) (2022-01-12)
Heart failure (HF) as a result of myocardial infarction (MI) is a major cause of fatality worldwide. However, the cause of cardiac dysfunction succeeding MI has not been elucidated at a sarcomeric level. Thus, studying the alterations within the sarcomere
T Kawai et al.
Molecular and cellular biology, 18(3), 1642-1651 (1998-03-06)
We have identified a novel serine/threonine kinase, designated ZIP kinase, which mediates apoptosis. ZIP kinase contains a leucine zipper structure at its C terminus, in addition to a kinase domain at its N terminus. ZIP kinase physically binds to ATF4
Mariko Takahashi et al.
Nature immunology, 22(4), 485-496 (2021-03-27)
Evasion of host immunity is a hallmark of cancer; however, mechanisms linking oncogenic mutations and immune escape are incompletely understood. Through loss-of-function screening of 1,001 tumor suppressor genes, we identified death-associated protein kinase 3 (DAPK3) as a previously unrecognized driver

Questions

Reviews

No rating value

Active Filters

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service