Analytical Data
-
Gene name
AAP
- Application
-
Alternative Names
AAP;PSA;Puromycin-sensitive aminopeptidase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P08697
-
Expression Region
40-491aa
-
AA Sequence
N QEQVSPLTLL KLGNQEPGGQ TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM EEDYPQFGSP K
-
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
AAP (Adenylate Cyclase-Activating Polypeptide) is a significant member of the vasoactive intestinal peptide (VIP) family, known for its diverse biological roles, including modulation of neuronal activity, neuroprotection, and influence on endocrine functions. Research into AAP has gained momentum due to its involvement in various physiological and pathological processes, such as stress response, circadian rhythm regulation, and inflammation. AAP’s receptor interactions lead to activation of intracellular signaling pathways, notably the cyclic AMP (cAMP) pathway, which plays a crucial role in cell signaling and function. Given its widespread effects on multiple organ systems and its potential therapeutic implications, AAP has become a target for drug development in treating conditions like neurodegenerative diseases, mood disorders, and metabolic syndrome. Investigations into the structure and function of recombinantly expressed AAP proteins have provided insights into their mechanisms and allowed for the development of novel therapeutics. Furthermore, the ability to produce AAP in a recombinant form has facilitated detailed studies into its post-translational modifications and stability, enhancing our understanding of its biological activity and therapeutic potential. This burgeoning field underscores the importance of AAP research in uncovering new avenues for clinical intervention and expanding our knowledge of neuropeptide biology.











