Recombinant Human Death Domain-Containing Protein Cradd (CRADD) Protein (His-SUMO)

Name: Recombinant Human Death Domain-Containing Protein Cradd (CRADD) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09924P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Death Domain-Containing Protein Cradd (CRADD) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P78560
Target Symbol	CRADD
Synonyms	CASP2 and RIPK1 domain containing adaptor with death domain ; Caspase and RIP adapter with death domain; Caspase and RIP adaptor with death domain ; Cradd; CRADD_HUMAN; Death adaptor molecule RAIDD ; Death domain containing protein CRADD ; Death domain-containing protein CRADD; MGC9163; RIP associated ICH1/CED3 homologous protein with death domain ; RIP associated protein with a death domain ; RIP-associated protein with a death domain
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEINAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLKKAREEAMTDLPAGDRLTGIPSHILNSSPSDRQINQLAQRLGPEWEPMVLSLGLSQTDIYRCKANHPHNVQSQVVEAFIRWRQRFGKQATFQSLHNGLRAVEVDPSLLLHMLE
Expression Range	1-199aa
Protein Length	Full Length
Mol. Weight	38.7kDa
Research Area	Apoptosis
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis. Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 2340 OMIM: 603454 KEGG: hsa:8738 STRING: 9606.ENSP00000327647 UniGene: PMID: 28686357 The megalencephaly, lissencephaly variant, and intellectual disability associated with loss of CRADD/caspase-2-mediated apoptosis imply a role for CRADD/caspase-2 signaling in development of the human cerebral cortex. PMID: 27773430 The adaptor molecule RAIDD coordinates IKKepsilon and IRF7 interaction to ensure efficient expression of type I interferon. PMID: 27606466 define a novel function for CRADD in endothelial cells as an inducible suppressor of BCL10, a key mediator of responses to proinflammatory agonists PMID: 24958727 Crystals are trigonal and belong to space group P3(1)21 (or its enantiomorph P3(2)21) with unit-cell parameters a = 56.3, b = 56.3, c = 64.9 A and gamma = 120 degrees . PMID: 19582216 Study identified sequence variants in the known disease-causing genes SLC6A3 and FLVCR1, and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1, SNIP1, CRADD, and HARS. PMID: 22279524 point mutations on RAIDD (R147E) and on PIDD (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed PMID: 20406701 The expressions of PIDD and RAIDD are upregulated during tumour progression in renal cell carcinomas. PMID: 20208132 As a first step towards elucidating the molecular mechanisms of caspase-2 activation, data report the crystal structure of the RAIDD death domain at 2.0 A resolution. PMID: 16434054 PIDD death domain (DD) and RAIDD DD assemble into an oligomeric complex. Within the PIDDosome, the interaction between PIDD and RAIDD is mediated by a homotypic interaction between their death domains. PMID: 17329820 impaired expression of RAIDD in drug induced apoptosis may play a role in the multidrug resistance of osteosarcoma cells PMID: 19125251

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.