Analytical Data
-
Gene name
PRPS1L1
- Application
-
Alternative Names
PRPS1L1; PRPS3; PRPSL; Ribose-phosphate pyrophosphokinase 3; EC 2.7.6.1; Phosphoribosyl pyrophosphate synthase 1-like 1; PRPS1-like 1; Phosphoribosyl pyrophosphate synthase III; PRS-III
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P21108
-
Expression Region
2-318 aa
-
AA Sequence
PNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIDESVRG EDVYIVQSGC GEINDSLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRSPISAK LVANMLSIAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPT VLKWIRENIP EWKNCIIVSP DAGGAKRVTS IADQLNVDFA LIHKERKKAN EVDCIVLVGD VNDRVAILVD DMADTCVTIC LAADKLLSAG ATRVYAILTH GIFSGPAISR INTACFEAVV VTNTIPQDEK MKHCSKIRVI DISMILAEAI RRTHNGESVS YLFSHVPL
-
Molecular Weight
34.8 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
PRPS1L1, a gene encoding a protein involved in nucleotide metabolism, has garnered attention in recent years due to its potential implications in various biological processes and diseases. It is a member of the ribose-phosphate pyrophosphokinase (PRPP synthase) family, which plays a crucial role in synthesizing phosphoribosyl pyrophosphate (PRPP), a key substrate in the biosynthesis of nucleotides and nucleic acids. The dysfunction of this pathway can lead to various disorders, including neurodegenerative diseases and certain types of cancer. Recent studies have suggested that PRPS1L1 may contribute to cellular responses to stress and play a role in the regulation of cell proliferation and survival. Understanding the structure and function of the PRPS1L1 recombinant protein can provide valuable insights into its biological role and therapeutic potential. By exploring its interaction with other cellular components and its regulation under different physiological conditions, researchers aim to elucidate the mechanistic pathways in which PRPS1L1 is involved. This knowledge could pave the way for novel therapeutic strategies targeting related metabolic pathways, ultimately improving the management of diseases associated with PRPS1L1 dysfunction. The study of PRPS1L1 recombinant protein is thus essential not only for basic scientific understanding but also for its potential translational applications in medicine.
