Analytical Data
-
Gene name
DPEP2
- Application
-
Alternative Names
DPEP2；Dipeptidase 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9H4A9-2
-
Expression Region
1-376aa
-
AA Sequence
MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RAQFWSAYVP CQTQDRDALR LTLEQIDLIR RMCASYSELE LVTSAKALND TQKLACLIGV EGGHSLDNSL SILRTFYMLG VRYLTLTHTC NTPWAESSAK GVHSFYNNIS GLTDFGEKVV AEMNRLGMMV DLSHVSDAVA RRALEVSQAP VIFSHSAARG VCNSARNVPD DILQLLKKNG GVVMVSLSMG VIQCNPSANV STVADHFDHI KAVIGSKFIG IGGDYDGAGK FPQGLEDVST YPVLIEELLS RGWSEEELQG VLRGNLLRVF RQVEKVQEEN KWQSPLEDKF PDEQLSSSCH SDLSRLRQRQ SLTSGQELTE IPIHWTAKLP AKWSVS
-
Molecular Weight
53 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
Dipeptidyl peptidase II (DPEP2) is a serine peptidase that plays a significant role in various physiological processes, including peptide metabolism and immune responses. The enzyme is primarily expressed in the gastrointestinal tract and has been implicated in the modulation of bioactive peptides, which are crucial for regulating numerous biological functions, such as inflammation and cell signaling. Research into DPEP2 has gained momentum due to its potential as a therapeutic target for diseases such as diabetes, cancer, and autoimmune disorders. Recombinant DPEP2 protein has been generated to facilitate detailed studies of its enzymatic activity, substrate specificity, and the structural basis of its function. The production of this recombinant protein enables the elucidation of the enzyme's role in peptide processing and its interactions with various substrates. Furthermore, understanding DPEP2's functions at a molecular level can aid in the design of specific inhibitors or modulators, paving the way for novel therapeutic strategies. The ongoing research on DPEP2 highlights the enzyme's significance in both basic and applied biomedical sciences, making it a focal point for future investigations into enzyme-linked pathways and their implications in health and disease.
