Analytical Data
-
Gene name
FNDC8
- Application
-
Alternative Names
FNDC8Fibronectin type III domain-containing protein 8
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8TC99
-
Expression Region
1-324aa
-
AA Sequence
MASEALHQVGDGEEAVLKKENFNMMNALDQLPKPFPNPKSMNRTVTTKGLPLASKGNLVNFLEDDTINLLKPLPVEDSDCSSDETSISAFSSTLLNPIKLAVTQPNSSFFAGMLEGELNKLSFSPMAKNAENEDLALGPCPCPSKSQMATRGLLDLDNPELETETSSTHSESSVVVDLPDTPFIFEHTVNNSTAVISWTYALGKQPVSFYQLLLQEVAKTQENELPEAKNRPWIFNKILGTTVKLMELKPNTCYCLSVRAANTAGVGKWCKPYKFATLATDFSSFPENYPIQITVRRKEPRQKIVSIGPEEMRRLEDLEYLFPC
-
Molecular Weight
62.3 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
FNDC8 (Fibronectin Type III Domain-Containing Protein 8) is a recently identified protein that plays a significant role in various biological processes, including muscle metabolism and energy regulation. Initial studies have highlighted its potential involvement in brown adipose tissue development and the regulation of thermogenesis, making it a candidate of interest for obesity and metabolic disorder research. The protein is thought to act as a signaling molecule, influencing cellular responses to physiological stimuli. Its structure, characterized by fibronectin type III domains, raises questions about its interaction with other molecules and its specific functional roles. Given the global rise in obesity-related health issues, understanding FNDC8's mechanisms could provide new therapeutic avenues for treating metabolic diseases. Furthermore, the potential link between FNDC8 and muscle function suggests its relevance in age-related muscle degeneration and conditions such as sarcopenia. As the field progresses, the characterization of recombinant FNDC8 protein can facilitate studies on its biological functions and therapeutic implications, thereby advancing our understanding of its role in metabolism and muscle physiology.
