Analytical Data
-
Gene name
PKLR
- Application
-
Alternative Names
Pyruvate kinase 1;Pyruvate kinase isozymes L/RR-type/L-type pyruvate kinaseRed cell/liver pyruvate kinase
-
Species
Human
-
Source
Yeast
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P30613
-
Expression Region
1-574aa
-
Molecular Weight
63.8 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
PKLR is a critical enzyme involved in the regulation of glycolysis and gluconeogenesis, specifically functioning in the conversion of phosphoenolpyruvate to pyruvate in the liver and erythrocytes. The PKLR gene encodes two isoforms of pyruvate kinase, M (muscle) and L (liver), which are produced through alternative splicing. The expression of these isoforms is tightly regulated and plays a significant role in metabolic adaptation during varying physiological states. Mutations in the PKLR gene are linked to pyruvate kinase deficiency, a hereditary condition leading to hemolytic anemia due to compromised red blood cell metabolism. Understanding the structure and function of PKLR and its isoforms is essential for developing therapeutic strategies for related disorders. Research into PKLR recombinant proteins focuses on elucidating the mechanism of action, substrate specificity, and regulatory pathways involved in its activity. Additionally, studying PKLR's role in metabolic diseases, cancer metabolism, and overall energy homeostasis provides insights into potential drug targets and therapies that can address metabolic dysfunctions. Given these factors, the production of PKLR recombinant proteins is crucial for advancing our understanding of its physiological roles and the implications of its dysregulation in various diseases.
