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Anti-csBAP31, clone 144-A8, Cat. No. MABC1710, is a mouse monoclonal antibody that detects B-cell receptor-associated protein 31 and has been tested for use in ELISA, Flow Cytometry, Immunoprecipitation, and Western Blotting.
More>>Anti-csBAP31, clone 144-A8, Cat. No. MABC1710, is a mouse monoclonal antibody that detects B-cell receptor-associated protein 31 and has been tested for use in ELISA, Flow Cytometry, Immunoprecipitation, and Western Blotting. Less<<
Empfohlene Produkte
Übersicht
Replacement Information
Description
Catalogue Number
MABC1710-100UL
Description
Anti-csBAP31 Antibody, clone 144-A8
Alternate Names
Cell surface B-cell receptor-associated protein 31
BCR-associated protein 31
Bap31
6C6-AG tumor-associated antigen
Protein CDM
p28
Background Information
B-cell receptor-associated protein 31 (UniProt: P51572; also known as BCR-associated protein 31, BAP31, 6C6-AG tumor-associated antigen, Protein CDM, p28) is encoded by the BCAP31 (also known as BAP31, DXS1357E) gene (Gene ID: 10134) in human. BAP31 is an endoplasmic reticulum (ER) membrane protein that is also expressed on surface (csBAP31) of embryonic stem cells. ER associated BAP1 palsy a significant role as a molecular chaperone for the newly synthesized transmembrane proteins and also acts as an important regulator of apoptosis. It interacts with pro-caspase-8L and Bcl-2/Bcl-xL on the ER membrane and is cleaved by caspase-8. The resulting cleaved product, p20, is an important inducer of apoptosis. The cell surface expressed BAP31 is shown to promote cell survival through the regulation of cell adhesion to the extracellular matrix in human embryonic stem cells. csBAP31 is also suggested to be a putative pro-apoptotic flag on cancer cells. Its expression is shown to be enhanced in caspase3/7 high A549 cells and csBAP31-positive cells display diminished survival capacity. Higher levels of csBAP31 are reported to contribute to poor survival cancer cells. Clone SP1-B7 specifically recognizes the cell surface-expressed BAP31. (Ref.: Seo, SR et al. (2017). PLoS One 12(11): e0188075).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-csBAP31, clone 144-A8, Cat. No. MABC1710, is a mouse monoclonal antibody that detects B-cell receptor-associated protein 31 and has been tested for use in ELISA, Flow Cytometry, Immunoprecipitation, and Western Blotting.
Key Applications
ELISA
Flow Cytometry
Immunoprecipitation
Western Blotting
Application Notes
Immunoprecipitation Analysis: A representative lot immunoprecipitated csBAP31 in Immunoprecipitation applications (Kim, WT., et. al. (2017). PLoS One. 12(1):e0170145).
Western Blotting Analysis: A representative lot detected csBAP31 in Western Blotting applications (Kim, WT., et. al. (2016). PLoS One. 11(12):e0167527; Kim, WT., et. al. (2017). PLoS One. 12(1):e0170145).
ELISA Analysis: A representative lot detected csBAP31 in ELISA applications (Kim, WT., et. al. (2016). PLoS One. 11(12):e0167527).
Flow Cytometry Analysis: A representative lot detected csBAP31 in Flow Cytometry applications (Kim, WT., et. al. (2016). PLoS One. 11(12):e0167527; Kim, WT., et. al. (2017). PLoS One. 12(1):e0170145).
Biological Information
Immunogen
H9 human embryonic stem cells pretreated with retinoic acid.
Clone
144-A8
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone 144-A8 is a mouse monoclonal antibody that detects human Cell surface B-cell receptor-associated protein 31 (csBAP31). It targets an epitope within 10 amino acids from the C-terminal region.
Flow Cytometry Analysis: 1 µg of this antibody detected csBAP31 in one million Ramos cells.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Molecular Characterization of Two Monoclonal Antibodies against the Same Epitope on B-Cell Receptor Associated Protein 31. Kim, WT; Shin, S; Hwang, HJ; Kim, MK; Jung, HS; Park, H; Ryu, CJ PLoS One
11
e0167527
2015
Previously, we showed that B-cell receptor associated protein 31 (BAP31), an endoplasmic reticulum (ER) membrane chaperone, is also expressed on the cell surface by two monoclonal antibodies (MAbs) 297-D4 and 144-A8. Both MAbs recognize the same linear epitope on the C-terminal domain of BAP31, although they were independently established. Here, flow cytometric analysis showed that 144-A8 had additional binding properties to some cells, as compared to 297-D4. Quantitative antigen binding assays also showed that 144-A8 had higher antigen binding capacity than 297-D4. Affinity measurement revealed that 144-A8 had 1.54-fold higher binding affinity than 297-D4. Analysis of the heavy- and light-chain variable region sequences of two MAbs revealed that both MAbs belonged to the same heavy chain (Igh-V3660 VH3) and light chain subgroup (IGKV21) with just two amino acid differences in each framework region, indicating that both MAbs arise from the same germline origin. Seven amino acid differences were found between the complementarity determining regions (CDRs) of the two MAbs. Molecular modeling of the epitope-paratope complexes revealed that the epitope appeared to reside in closer proximity to the CDRs of 144-A8 than to those of 297-D4 with the stronger hydrogen bond interactions with the former than the latter. More interestingly, an additional hydrophobic interaction appeared to be established between the leucine residue of epitope and the paratope of 144-A8, due to the substitution of H-Tyr101 for H-Phe101 in 144-A8. Thus, the different binding specificity and affinity of 144-A8 appeared to be due to the different hydrogen bonds and hydrophobic interaction induced by the alterations of amino acids in CDRs of 144-A8. The results provide molecular insights into how the binding specificities and affinities of antibodies evolve with the same epitope in different microenvironments.
Correction: Epitope Mapping of Antibodies Suggests the Novel Membrane Topology of B-Cell Receptor Associated Protein 31 on the Cell Surface of Embryonic Stem Cells: The Novel Membrane Topology of BAP31. Kim, WT; Choi, HS; Hwang, HJ; Jung, HS; Ryu, CJ PLoS One
12
e0170145
2001
