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Mouse Anti-Porcine Pleckstrin (PLEK) Monoclonal Antibody

Cat. No.VD8N382

Product TypeAnimal-targeted Antibodies

Size

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Product Overview

BioVenic mouse monoclonal antibody is specific for pleckstrin. It is affinity purified by protein G. It can be applied to WB, IF, IHC and ELISA assays of pleckstrin.

Specifications

Application WB; IF; IHC; ELISA

Clonality Monoclonal

Classification Primary Antibody

Clone G8N35

Host Mouse

Target Species Porcine

Species Reactivity Porcine

Specificity Pleckstrin

Isotype IgG1

Immunogen Recombinant protein of pleckstrin

Purification Protein G Purified

Concentration 1600 μg/mL

Conjugation Unconjugated

Preservative and Stabilizer 0.02% Sodium Azide

Buffer Phosphate Buffered Saline with 50% Glycerol, pH 7.3

Physical State Liquid

Target Information

Porcine pleckstrin (pPLEK), a member of the pleckstrin family of proteins, is an important component in cellular signal transduction pathways, particularly those involving phosphoinositide binding. pPLEK plays a crucial role in various cellular processes, including cell signaling, cytoskeletal rearrangement, and membrane trafficking. This protein is known for its ability to bind to phosphatidylinositol (PI) lipids, which are key regulators of cellular functions. The interaction of pPLEK with these lipids is often mediated by its pleckstrin homology (PH) domain, allowing it to participate in the regulation of multiple signaling cascades.

Target Pleckstrin

Target Synonym P47; Platelet 47 kDa protein

Gene ID 100516257

UniProt ID A0A5G2QT56

Shipping and Storage

This product is shipped with ice gel packs. Store at -20°C (up to 12 months) on receipt.

Documents

Datasheet

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

Kohn, Aimee D., et al. "Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation." Journal of Biological Chemistry 271.36 (1996): 21920-21926.