Recombinant Human CRADD protein(Met1-Glu199), His-tagged

• Cat.No.: CRADD-6914H
• Product Overview: Recombinant Human CRADD (P78560) (Met 1-Glu 199) was expressed in E. coli, fused with a polyhistidine tag at the C-terminus.

Specification

• Species: Human
• Source: E.coli
• Tag: His
• Protein Length: Met1-Glu199
• Form: Lyophilized from sterile PBS, 20% glycerol, pH 8.0. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human CRADD consisting of 209 amino acids and has a calculated molecular mass of 24.1 kDa. It migrates as an approximately 26 kDa band in SDS-PAGE under reducing conditions.
• Purity: > 95 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: CRADD CASP2 and RIPK1 domain containing adaptor with death domain [ Homo sapiens ]
• Official Symbol: CRADD
• Synonyms: CRADD; CASP2 and RIPK1 domain containing adaptor with death domain; death domain-containing protein CRADD; RAIDD; RIP associated ICH1/CED3 homologous protein with death domain; death adaptor molecule RAIDD; caspase and RIP adaptor with death domain; RIP-associated protein with a death domain; RIP-associated ICH1/CED3-homologous protein with death domain; MRT34; MGC9163
• Gene ID: 8738
• mRNA Refseq: NM_003805
• Protein Refseq: NP_003796
• MIM: 603454
• UniProt ID: P78560

Case Study

Case 1: Qiao H, et al. J Biol Chem. 2014

Increased blood vessel permeability is a key feature of inflammation, triggered in endothelial cells by proteins like BCL10. However, CRADD helps keep this in check. In mouse endothelial cells missing CRADD, inflammation escalates with disrupted cell junctions, making the vessels leakier. By introducing a special CRADD protein, researchers could restore normal function, reducing inflammation and reinforcing cell barriers, even in healthy cells. This highlights CRADD's crucial role in controlling inflammation and maintaining blood vessel stability.

Fig1. Protein staining with Coomassie Blue displays recombinant non-CP-CRADD (25 kDa) and CP-CRADD (26 kDa) proteins.

Fig2. LMEC isolated from cradd−/− mice were treated for 3 h with equimolar doses (12 μm) of non-CP-CRADD or CP-CRADD, then stimulated with LPS.

Case 2: Maney SK, et al. Cell Physiol Biochem. 2016

Viral infections are a big health issue worldwide, pushing us to find new treatments and understand immune responses better. Our body's quick response includes making type I interferon (IFN-I) right after spotting a virus, though the precise signaling pathways remain a bit of a mystery. This study reveals that the CRADD protein is crucial in this process. It interacts with proteins IRF7 and IKKε, essential for IFN-I production. When CRADD is missing, IFN-I levels drop dramatically, and tweaking specific parts of CRADD further disrupts interferon activation, highlighting its vital role in our antiviral defenses.

Fig1. Whole cell lysates were prepared from HEK TLR3 cells expressing scrRNA and shRNA RAIDD at indicated time points and probed for RAIDD and β actin.

Fig2. 293t cells were lysed followed by immunoprecipitation (IP) using anti-FLAG (RAIDD).

Application

Recombinant CRADD protein is opening up exciting possibilities in both research and treatment arenas. By recreating this protein in the lab, researchers can explore its crucial roles, like controlling inflammation and cell death, without interfering with natural protein functions in the body. Picture having a specific tool to understand how CRADD manages immune reactions, especially in autoimmune disorders where the body's defenses mistakenly target its own cells. This understanding could lead to new, smarter therapies with fewer side effects, offering significant relief. On the treatment side, recombinant CRADD holds a lot of promise. In diseases where inflammation runs wild or cells die off abnormally, like in some cancers or inflammatory conditions, this protein might help bring things back into balance. By delivering it right to the problem areas, scientists hope to use its natural abilities to calm inflammation and regulate how cells decide to live or die. This approach could result in treatments that are not only more effective but also tailored to what each patient truly needs. Such advances in biotechnology demonstrate how we are moving towards solutions that can tackle tough health challenges in more personalized ways.

Fig1. Downregulation of p53-induced death domain protein (PIDD)-osome components by different inhibitors that could be used in the therapy of neurodegeneration diseases. (Pavel I Volik, 2023)