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BAP31 monoclonal antibody (A1/182)

 
ALX-804-601-C100 100 µg 334.00 USD
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Product Specification

Alternative Name:p28 BAP31, B cell receptor-associated protein BAP31, BCR-associated protein BAP31, CDM, DXS1357E, 6C6-AG tumor-associated antigen, BCAP31
 
Clone:A1/182
 
Host:Mouse
 
Isotype:IgG2a
 
Immunogen:BAP31 (BCR associated protein BAP031) from Vero monkey cells.
 
UniProt ID:P51572 (human)
 
Species reactivity:Human
Monkey
 
Applications:ELISA, Flow Cytometry, ICC, IHC (FS), IP, WB
 
Recommended Dilutions/Conditions:Immunocytochemistry (1:1,000)
Immunoprecipitation (2µl)
Western Blot (1:1,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Formulation:Lyophilized. Protein G-affinity purified and gel filtrated (FPLC).
 
Reconstitution:Reconstitute with 100µl PBS containing 0.1% sodium azide.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background:BAP31 (B cell receptor-associated protein 31) is an integral protein of the ER membrane that forms a large hetero-oligomeric complex with the related BAP29. The cytosolic domain of BAP31 contains two identical caspase recognition sites that are preferentially cleaved by initiator caspases, including caspase-8. After activation of cell surface death receptors, human BAP31 is cleaved into a membrane-embedded fragment called p20, which induces apoptosis when expressed ectopically. The p20 fragment can mediate Ca2+-dependent apoptotic cross-talk between the ER and mitochondria, stimulating cytochrome c release. In addition to its role in apoptosis, BAP31 is a component of the ER quality control compartment and functions as a cargo receptor for ER export of transmembrane proteins such as cellubrevin, MHC class I molecules, and cytochrome P450 2C2.
 
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Product Literature References

Rhomboid intramembrane protease RHBDL4 triggers ER-export and non-canonical secretion of membrane-anchored TGFα: L. Wunderle, et al.; Sci. Rep. 6, 27342 (2016), Application(s): Immunofluorescence, Abstract; Full Text
Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution: A. Chadrin, et al.; J. Cell. Biol. 189, 795 (2010), Abstract;
Selective export of human GPI-anchored proteins from the endoplasmic reticulum: C. Bonnon, et al.; J. Cell Sci. 123, 1705 (2010), Abstract;
The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi: S. Mitrovic, et al.; Mol. Biol. Cell 19, 1976 (2008), Abstract;
Capturing protein interactions in the secretory pathway of living cells: B. Nyfeler, et al.; PNAS 102, 6350 (2005), Abstract; Full Text
Proteomics of endoplasmic reticulum-golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46: L. Breuza, et al.; J. Biol. Chem. 279, 47242 (2004), Abstract; Full Text
Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment: D.R. Klopfenstein, et al.; J. Cell Biol. 153, 1287 (2001), Abstract; Full Text
A novel direct interaction of endoplasmic reticulum with microtubules: D.R. Klopfenstein, et al.; EMBO J. 17, 6168 (1998), Abstract; Full Text
The recycling pathway of protein ERGIC-53 and dynamics of the ER-Golgi intermediate compartment: J. Klumperman, et al.; J. Cell Sci. 111, 3411 (1998), Abstract; Full Text

General Literature References

Bap31 Is an Itinerant Protein that Moves between the Peripheral ER and a Juxtanuclear Compartment Related to ER-associated Degradation: Y. Wakana, et al.; Mol. Biol. Cell 19, 1825 (2008), Abstract; Full Text
Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol: D.G. Breckenridge, et al.; J. Cell. Biol. 160, 1115 (2003), Abstract; Full Text
Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria: M. Nguyen, et al.; Mol. Cell. Biol. 20, 6731 (2000), Abstract; Full Text

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