Human CASP2 And RIPK1 Domain Containing Adaptor With Death Domain (CRADD) Protein

Este producto es parte de CRADD - Death domain-containing protein CRADD
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1235€ (100 µg)

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935106861
info@markelab.com
name
Human CASP2 And RIPK1 Domain Containing Adaptor With Death Domain (CRADD) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx692373
tested applications
SDS-PAGE

Description

Human CRADD Protein is a recombinant protein from Human produced in E. coli. A DNA sequence encoding the human CRADD (P78560) (Met 1-Glu 199) was fused with a polyhistidine tag at the C-terminus.

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Proteins and Peptides
Immunogen Target
CRADD
Host
E. coli
Origin
Human
Observed MW
Molecular Weight: 24.1 kDa
Sequence Fragment: Met1-Glu199
Tag: C-terminal His tag
Validity: The validity for this protein is 12 months.
Expression
Recombinant
Purity
> 95% (SDS-PAGE)
Size 1
100 µg
Form
 
Tested Applications
SDS-PAGE
Buffer
Lyophilized from sterile PBS, 20% glycerol, pH 8.0.
Availability
Shipped within 5-15 working days.
Storage
Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
P78560
Alias
RAIDD, MRT34,CASP2,RIPK1,CRADD
Background
Protein CRADD
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Death domain-containing protein CRADD, also known as RIP, is involved in mediating cellular responses to stress, particularly in the regulation of apoptosis. It contains a death domain (DD) and serves as a key adaptor protein in the signaling pathways triggered by death receptors. CRADD is known to participate in the formation of the death-inducing signaling complex (DISC) when activated by signals such as tumor necrosis factor (TNF) or Fas ligand (FasL), leading to the activation of caspases and subsequent apoptosis. In addition, CRADD has been implicated in other processes, such as inflammation and neurodegeneration. Its expression and function are tightly regulated and have been linked to both cell survival and death in different contexts.

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