Analytical Data
-
Gene name
SURF4
- Application
-
Alternative Names
SURF4; SURF-4; Surfeit locus protein 4
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O15260
-
Expression Region
1-269 aa
-
AA Sequence
MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWNCGYLLASSFVFLNLLGQLTGCVLVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSIVQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW
-
Molecular Weight
56.8 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
SURF4 (Surfeit 4) is a protein associated with the endoplasmic reticulum and plays a significant role in the trafficking and processing of glycoproteins. Its involvement in various cellular processes, including protein folding and quality control, has sparked research interest, particularly in the context of neurodegenerative diseases and metabolic disorders. Recent studies have suggested that dysfunction or mislocalization of SURF4 may contribute to these disease mechanisms, making it an attractive target for therapeutic intervention. Additionally, the understanding of SURF4’s structural and functional properties can provide insights into the molecular pathways governing cellular homeostasis. Advanced techniques such as recombinant protein expression and purification have become pivotal in characterizing SURF4, facilitating the exploration of its physiological roles and interactions with other cellular components. The ongoing research into SURF4 aims to unravel its biological significance and potential implications in health and disease, paving the way for novel diagnostic and treatment strategies. As scientists continue to investigate the intricacies of SURF4, the hope is to link its function to broader therapeutic applications in conditions where protein misfolding and trafficking are prominent.
