PACAP-SAP [IT-84, KIT-84]

Name: PACAP-SAP [IT-84, KIT-84]
SKU: IT-84
Availability: InStock

a tool for eliminating cells that express VPAC1, VPAC2, or PAC1 receptors; targeted via biotinylated PACAP, eliminated via saporin

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SKU: IT-84 Category: Targeted Toxins Quantity: Individual 25 ug, Individual 100 ug, Individual 250 ug, Individual 1 mg, Kit w/controls 25 ug, Kit w/controls 100 ug, Kit w/controls 250 ug | Conjugate: streptavidin-saporin | Usage: eliminates cells |

Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38 amino acid neurotrophic factor that is involved in a wide range of nervous system functions including development, differentiation, stress responses, and various aspects of learning and memory. PACAP binds with high affinity to PAC1, VPAC1 and VPAC2 receptors. The PACAP-specific PAC1 receptor is expressed in many places, including: the adrenal medulla, pancreatic acini, uterus, myenteric plexus, trigeminal ganglia, otic ganglia, superior cervical ganglia (pre junctional) and cerebral arteries (post junctional). PAC1 has also been shown to be expressed by non-squamous lung cancer and breast cancer cell lines, and plays a role in the regulation of growth and proliferation of these cells. VPAC receptors display comparable affinity for vasoactive intestinal peptide (VIP) and PACAP. The VPAC receptors are expressed in the central nervous system, pancreas, skeletal muscle, heart, kidney, adipose tissue, testis and stomach. PACAP-SAP eliminates cells that express PAC1, VPAC1, or VPAC2 receptors. PACAP-SAP can be used as an effective tool in your research to study the effects of the absence of these cells in circadian rhythm, heart failure, various aspects of the digestive system, neurological disorders such as PTSD, and paracrine and autocrine regulation of certain cell types.

PACAP-SAP is a bonded toxin between biotinylated pituitary adenylate cyclase activating peptide and the secondary conjugate Streptavidin-ZAP containing the ribosome-inactivating protein, saporin. It specifically eliminates cells expressing VPAC1, VPAC2, or PAC1 receptors.

PACAP-SAP is available individually (Cat. #IT-84) or as a kit (Cat. #KIT-84) which includes PACAP-SAP and Blank-Streptavidin-SAP (Cat. #IT-27B).

keywords: PACAP, VIP, pituitary adenylate cyclase-activating polypeptide neurotrophic factor, vasoactive intestinal peptide, VPAC, VPAC1, VPAC2, PAC1, streptavidin, saporin, learning, memory, circadian rhythm, heart failure, digestive system, PTSD, brain, neuroscience

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Pituitary adenylate cylase-activating polypeptide receptor: Multiple signaling pathways involved in energy homeostasis

Maunze B (2022) Pituitary adenylate cylase-activating polypeptide receptor: Multiple signaling pathways involved in energy homeostasis. Marquette University Dissertations 1212. Thesis.

Objective: To determine the endogenous role of pituitary adenylate cyclase activating polypeptide (PACAP) in affecting the ventromedial nuclei (VMN) of the hypothalamus and its control of feeding and energy expenditure through the Type I PAC1 receptor (PAC1R).

Summary: VMN cells expressing PAC1 receptors in Male Sprague Dawley rats were knocked down via injection of Saporin or PACAP-SAP and trafficking also pharmacologically inhibited. This increased meal sizes, reduced total number of meals, and induced body weight gain. PACAP signaling replicates the effects of leptin administration in the VMN and appears to enable leptin regulation of energy homeostasis. Co-immunoprecipitation was used to show that VMN PAC1 and leptin receptors are found in the same cell, and they form an immunocomplex. Inhibiting downstream effectors of PACAP signaling, such as PKA and PKC, enhanced or prevented leptin signaling respectively. The current findings revealed that endogenous PACAP signaling in the VMN has a potent regulatory influence over both energy intake in the form of feeding, and energy output via thermogenesis and locomotor activity. Moreover, PACAP actions in the VMN share nearly identical secondary effects as with leptin administration in the same brain region suggesting that these two neuropeptides could functionally intersect.

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