|Other Names||Large proline-rich protein BAG6, BAG family molecular chaperone regulator 6, BCL2-associated athanogene 6, BAG-6, BAG6, HLA-B-associated transcript 3, Protein G3, Protein Scythe, BAG6, BAT3, G3|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. Moreover, it regulates the stability and the degradation of proteins by the proteasome. For instance, it is required for selective ubiquitin- mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno- proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. It is also involved in ubiquitin-mediated proteasomal degradation of proteins of the secretory pathway that are mislocalized to the cytosol. Binds the mislocalized proteins, preventing their aggregation in the cytosol, and promotes their ubiquitination. Participates in endoplasmic reticulum stress- induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2.|
|Cellular Location||Cytoplasm, cytosol. Nucleus. Note=The C- terminal fragment generated by caspase-3 is cytoplasmic. Also found in extracellular vesicular exosomes in some tumor cells|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
This gene was first characterized as part of a cluster ofgenes located within the human major histocompatibility complexclass III region. This gene encodes a nuclear protein that iscleaved by caspase 3 and is implicated in the control of apoptosis.In addition, the protein forms a complex with E1A binding proteinp300 and is required for the acetylation of p53 in response to DNAdamage. Multiple transcript variants encoding different isoformshave been found for this gene.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Ucisik-Akkaya, E., et al. Mol. Hum. Reprod. 16(10):770-777(2010)Minami, R., et al. J. Cell Biol. 190(4):637-650(2010)Liu, C.Y., et al. Carcinogenesis 31(7):1259-1263(2010)Hsieh, Y.Y., et al. J. Clin. Lab. Anal. 24(4):262-268(2010)
If you have used an Abgent product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at firstname.lastname@example.org.