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Key Documents

COO/COA

SRP0418

WDR5 human

Name: WDR5 human
Brand: SIGMA

recombinant, expressed in baculovirus infected Sf9 cells, ≥90% (SDS-PAGE)

Synonym(s):

BIG-3, SWD3, WD Repeat Domain 5

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About This Item

UNSPSC Code:

12352202

NACRES:

NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

assay

≥90% (SDS-PAGE)

form

aqueous solution

mol wt

37.5 kDa

packaging

pkg of 100 μg

NCBI accession no.

NM_017588

UniProt accession no.

P61964

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... WDR5(11091)

General description

Human WDR5 (WD Repeat Domain 5), also known as SWD3 or BIG-3 (GenBank Accession No. NM_017588) amino acids 2-334 (end) with N-terminal His-tag, MW=37.5 kDa, expressed in Sf9 insect cells via a Baculovirus expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

pictograms

GHS08,GHS07

signalword

Danger

hcodes

H315,H319,H360D

pcodes

P202 - P264 - P280 - P302 + P352 - P305 + P351 + P338 - P308 + P313

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

Storage Class

6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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WDR5, a complexed protein.

Raymond C Trievel et al.

Nature structural & molecular biology, 16(7), 678-680 (2009-07-07)

WDR5 is essential for assembly of the VISA-associated signaling complex and virus-triggered IRF3 and NF-kappaB activation.

Yan-Yi Wang et al.

Proceedings of the National Academy of Sciences of the United States of America, 107(2), 815-820 (2010-01-19)

Viral infection causes activation of the transcription factors NF-kappaB and IRF3, which collaborate to induce type I interferons (IFNs) and cellular antiviral response. The mitochondrial outer membrane protein VISA acts as a critical adapter for assembling a virus-induced complex that

Characterization of a novel WDR5-binding site that recruits RbBP5 through a conserved motif to enhance methylation of histone H3 lysine 4 by mixed lineage leukemia protein-1.

Zain Odho et al.

The Journal of biological chemistry, 285(43), 32967-32976 (2010-08-19)

Histone modification is well established as a fundamental mechanism driving the regulation of transcription, replication, and DNA repair through the control of chromatin structure. Likewise, it is apparent that incorrect targeting of histone modifications contributes to misregulated gene expression and

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