VIPR2 Protein, Human (HEK293, Fc)

VIPR2 protein, serving as a receptor for Vasoactive Intestinal Peptide (VIP) and Pituitary Adenylate Cyclase-Activating Peptide (PACAP-38 and -27), activates adenylyl cyclase and can also couple with phospholipase C. Its versatile signaling pathways emphasize its pivotal role in transducing signals from VIP and PACAP, participating in cellular processes regulated by cyclic AMP and phosphoinositide signaling cascades. VIPR2 Protein, Human (HEK293, Fc) is the recombinant human-derived VIPR2 protein, expressed by HEK293 , with C-mFc labeled tag.

The VIPR2 protein functions as a receptor for Vasoactive Intestinal Peptide (VIP) as well as Pituitary Adenylate Cyclase-Activating Peptide (PACAP-38 and -27). The receptor's activity is mediated by G proteins, leading to the activation of adenylyl cyclase. Additionally, VIPR2 exhibits the capability to couple with phospholipase C, showcasing its versatility in signaling pathways. These interactions highlight the pivotal role of VIPR2 in transducing signals from VIP and PACAP, thereby participating in cellular processes regulated by cyclic AMP and phosphoinositide signaling cascades.

Human

HEK293

C-mFc

P41587 (E24-V126)

7434  [NCBI]

Partial

ECRFHLEIQEEETKCAELLRSQTEKHKACSGVWDNITCWRPANVGETVTVPCPKVFSNFYSKAGNISKNCTSDGWSETFPDFVDACGYSDPEDESKITFYILV

Approximately 45-60 kDa, based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.