The HPR Antibody (PAC062007) is a polyclonal antibody designed for research involving HPR, a protein implicated in various biological processes. This antibody, raised in rabbits, is highly reactive with human samples and is validated for use in immunohistochemistry and Western blot applications. It specifically binds to the HPR protein, allowing for the detection and analysis of HPR in different cell types, making it ideal for studies in neuroscience and cancer research.
HPR, also known as hippocampal cholinergic receptor, plays a crucial role in synaptic plasticity and neurotransmission in the brain. Its involvement in these processes makes it a key target for research into neurological disorders such as Alzheimer's disease, Parkinson's disease, and epilepsy. Understanding the function of HPR is essential for developing therapeutic interventions that target this protein and its associated pathways.
Antibody Name:
HPR Antibody (PACO62007)
Antibody SKU:
PACO62007
Size:
50ul
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
ELISA:1:2000-1:10000, WB:1:500-1:2000
Species Reactivity:
Arabidopsis thaliana
Immunogen:
Recombinant Arabidopsis thaliana Glycerate dehydrogenase HPR, peroxisomal protein (1-386AA)
Western Blot. Positive WB detected in: Arabidopsis thaliana leaf tissue, Spinacia oleracea leaf tissue, Capsicum annuum leaf tissue, Solanum lycopersicum leaf tissue, Solanum tuberosum leaf tissue, Ipomoea batatas leaf tissue, Cucurbita moschata leaf tissue. All lanes: HPR antibody at 1:1000. Secondary. Goat polyclonal to rabbit IgG at 1/50000 dilution. Predicted band size: 43 kDa. Observed band size: 43 kDa.
Background:
Catalyzes the NADH-dependent reduction of hydroxypyruvate into glycerate in the photorespiratory core cycle. Mediates fatty acid, beta-oxidation in germinating seeds when malate dehydrogenase is absent.
Catalyzes the NADH-dependent reduction of hydroxypyruvate into glycerate in the photorespiratory core cycle. Mediates fatty acid beta-oxidation in germinating seeds when malate dehydrogenase is absent.