Analytical Data
-
Gene name
LHPP
- Application
-
Alternative Names
LHPP;Phospholysine phosphohistidine inorganic pyrophosphate phosphatase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9H008
-
Expression Region
1-270aa
-
AA Sequence
MRGSHHHHHP WYASMTGGQQ MGRDLYDDDD KDRWGSHMAP WGKRLAGVRG VLLDISGVLY DSGAGGGTAI AGSVEAVARL KRSRLKVRFC TNESQKSRAE LVGQLQRLGF DISEQEVTAP APAACQILKE QGLRPYLLIH DGVRSEFDQI DTSNPNCVVI ADAGESFSYQ NMNNAFQVLM ELEKPVLISL GKGRYYKETS GLMLDVGPYM KALEYACGIK AEVVGKPSPE FFKSALQAIG VEAHQAVMIG DDIVGDVGGA QRCGMRALQV RTGKFRPSDE HHPEVKADGY VDNLAEAVDL LLQHADK
-
Molecular Weight
34 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
LHPP (phospholysine phosphohistidine inorganic pyrophosphatase) is a novel enzyme that has garnered attention in recent years due to its unique role in cellular signaling and metabolism. It was initially discovered as a novel gene linked to various physiological processes and diseases, including cancer, where altered expression is often observed. The primary function of LHPP is to hydrolyze phospholysine and phosphohistidine residues, which plays a crucial role in regulating protein phosphorylation states and thus modulating cellular functions. Researchers are particularly interested in LHPP due to its potential as a therapeutic target; its dysregulation has been implicated in various pathologies, including tumorigenesis and neurodegenerative disorders. The study of recombinant LHPP proteins has advanced our understanding of its enzymatic mechanisms and substrate specificity, allowing for the development of inhibitors or modulators that could be used in disease treatment. Furthermore, advances in structural biology have paved the way for elucidating the three-dimensional conformation of LHPP, which is essential for rational drug design. Overall, the exploration of LHPP and its recombinant proteins offers promising avenues for therapeutic interventions and contributes to our understanding of its fundamental biological roles.
