Analytical Data
-
Gene name
NARF
- Application
-
Alternative Names
NARF；Nuclear prelamin A recognition factor
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UHQ1
-
Expression Region
1-456aa
-
AA Sequence
MKCEHCTRKE CSKKTKTDDQ ENVSADAPSP AQENGEKGEF HKLADAKIFL SDCLACDSCM TAEEGVQLSQ QNAKDFFRVL NLNKKCDTSK HKVLVVSVCP QSLPYFAAKF NLSVTDASRR LCGFLKSLGV HYVFDTTIAA DFSILESQKE FVRRYRQHSE EERTLPMLTS ACPGWVRYAE RVLGRPITAH LCTAKSPQQV MGSLVKDYFA RQQNLSPEKI FHVIVAPCYD KKLEALQESL PPALHGSRGA DCVLTSGEIA QIMEQGDLSV RDAAVDTLFG DLKEDKVTRH DGASSDGHLA HIFRHAAKEL FNEDVEEVTY RALRNKDFQE VTLEKNGEVV LRFAAAYGFR NIQNMILKLK KGKFPFHFVE VLACAGGCLN GRGQAQTPDG HADKALLRQM EGIYADIPVR RPESSAHVQE LYQEWLEGIN SPKAREVLHT TYQSQERGTH SLDIKW
-
Molecular Weight
51.1 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
NARF (NAD+ Replenishing Factor) is an essential protein that plays a significant role in cellular metabolism and energy homeostasis. Its function is closely linked to the regulation of NAD+ levels, a crucial coenzyme involved in various metabolic processes, including glycolysis, the citric acid cycle, and oxidative phosphorylation. As NAD+ levels decline with age and certain disease states, understanding the mechanisms underlying NARF's activity has garnered increasing interest among researchers. Studies indicate that NARF is involved in the modulation of cellular responses to stress, inflammation, and metabolic disorders. Furthermore, it has been implicated in age-related diseases, such as neurodegenerative disorders and metabolic syndromes, highlighting its potential as a therapeutic target. Research into the structural and functional aspects of NARF is vital to elucidating its role in maintaining cellular NAD+ homeostasis and its broader implications in health and disease. Advances in recombinant protein technology have paved the way for the production of NARF in vitro, allowing for detailed biochemical studies to investigate its interactions, enzymatic activities, and potential regulatory mechanisms. As a result, exploring NARF in the context of energy metabolism and cellular aging may lead to novel insights into disease prevention and intervention strategies that leverage the modulation of NAD+ levels in various pathological states.
