Analytical Data
-
Gene name
MEFV
- Application
-
Alternative Names
FMF; Marenostrin; Mediterranean fever; Mediterranean fever protein; MEF; Mefv; MEFV_HUMAN; Pyrin; TRIM20
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O15553
-
Expression Region
375-781aa
-
AA Sequence
CKRHLKQVQLLFCEDHDEPICLICSLSQEHQGHRVRPIEEVALEHK KKIQKQLEHLKKLRKSGEEQRSYGEEKAVSFLKQTEALKQRVQRKLEQVYYFLEQQEHFF VASLEDVGQMVGQIRKAYDTRVSQDIALLDALIGELEAKECQSEWELLQDIGDILHRAKT VPVPEKWTTPQEIKQKIQLLHQKSEFVEKSTKYFSETLRSEMEMFNVPELIGAQAHAVNV ILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVG DKTAWILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGI FVDYRVGSISFYNVTARSHIYTFASCSFSGPLQPIFSPGTRDGGKNTAPLTICPVGGQGPD
-
Molecular Weight
86,4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MEFV, the gene responsible for familial Mediterranean fever (FMF), encodes for the protein pyrin, which plays a crucial role in the regulation of inflammation and the innate immune response. Mutations in the MEFV gene are linked to FMF, a hereditary autoinflammatory disorder characterized by recurrent episodes of fever and serositis. Research into MEFV recombinant proteins aims to elucidate the functional mechanisms of pyrin, particularly how it interacts with other proteins in the inflammasome pathway, which is crucial for the activation of pro-inflammatory cytokines like IL-1β. Understanding the structure and function of the MEFV protein can provide insights into the pathophysiology of FMF and similar autoinflammatory conditions. Moreover, investigating MEFV-derived recombinant proteins holds potential for therapeutic applications, such as the development of targeted biologics that could alleviate the symptoms of FMF or other related disorders by modulating the inflammatory response. Recent advancements in molecular biology techniques have facilitated the production and characterization of recombinant MEFV proteins, enabling detailed studies of their biochemical properties and interactions. This line of research is pivotal for developing innovative treatment strategies and improving patient outcomes for individuals afflicted with FMF and related inflammatory diseases.











