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Mouse Anti-DNAJB6 Recombinant Antibody (2C11-C1) (CBMAB-D1297-YC)

Provided herein is a Mouse monoclonal antibody, which binds to DnaJ Heat Shock Protein Family (Hsp40) Member B6 (DNAJB6). The antibody can be used for immunoassay techniques, such as IF, WB.
See all DNAJB6 antibodies
Published Data
Fig.1 DNAJB6(S) inhibits p18 Bax cleavage and caspase-9 activation in MPP⁺⁻ treated cells.
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Fig.2 DNAJB6(S) transient overexpression protects against MPP⁺⁻ induced apoptosis.
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Fig.3 DNAJB6(S) prevents the loss of mitochondrial membrane potential (Δψm) in MPP⁺⁻ treated cells.
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Fig.4 H&E staining (upper panel) and transmission electron microscopic analysis (lower panel) of mouse myocardium at 3 months after DOX injection with or without AAV9-Dnajb6(L) preinjection.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
2C11-C1
Antibody Isotype
IgG1, κ
Application
IF, WB

Basic Information

Immunogen
DNAJB6 (AAH00177, 1 a.a. ~ 242 a.a) full length recombinant protein with GST tag.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
DnaJ Heat Shock Protein Family (Hsp40) Member B6
Introduction
DNAJB6 belongs to the DNAJ protein family. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. This family member may also play a role in polyglutamine aggregation in specific neurons. Alternative splicing of this gene results in multiple transcript variants; however, not all variants have been fully described.
Entrez Gene ID
10049
UniProt ID
O75190
Alternative Names
DnaJ Heat Shock Protein Family (Hsp40) Member B6; DnaJ (Hsp40) Homolog, Subfamily B, Member 6; Heat Shock Protein J2; HSJ-2; HHDJ1; MSJ-1; HSJ2; MRJ; Limb Girdle Muscular Dystrophy 1D (Autosomal Dominant);
Function
Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.
Biological Process
Actin cytoskeleton organization Source: Ensembl
Chorio-allantoic fusion Source: Ensembl
Chorion development Source: Ensembl
Extracellular matrix organization Source: Ensembl
Intermediate filament organization Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Negative regulation of inclusion body assembly Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: Ensembl
Protein folding Source: UniProtKB
Protein localization to nucleus Source: Ensembl
Regulation of cellular response to heat Source: Reactome
Regulation of protein localization Source: ParkinsonsUK-UCL
Syncytiotrophoblast cell differentiation involved in labyrinthine layer development Source: Ensembl
Cellular Location
Nucleus; Perinuclear region; Z line
Involvement in disease
Muscular dystrophy, limb-girdle, autosomal dominant 1 (LGMDD1):
The disease is caused by variants affecting the gene represented in this entry. There is evidence that LGMDD1 is caused by dysfunction of isoform B (PubMed:22366786). An autosomal dominant myopathy characterized by adult onset of proximal muscle weakness, beginning in the hip girdle region and later progressing to the shoulder girdle region.

Österlund, N., Lundqvist, M., Ilag, L. L., Gräslund, A., & Emanuelsson, C. (2020). Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation. Journal of Biological Chemistry, 295(24), 8135-8144.

Palmio, J., Jonson, P. H., Inoue, M., Sarparanta, J., Bengoechea, R., Savarese, M., ... & Udd, B. (2020). Mutations in the J domain of DNAJB6 cause dominant distal myopathy. Neuromuscular Disorders, 30(1), 38-46.

Thiruvalluvan, A., de Mattos, E. P., Brunsting, J. F., Bakels, R., Serlidaki, D., Barazzuol, L., ... & Kampinga, H. H. (2020). DNAJB6, a key factor in neuronal sensitivity to amyloidogenesis. Molecular cell, 78(2), 346-358.

Rodríguez-González, C., Lin, S., Arkan, S., & Hansen, C. (2020). Co-chaperones DNAJA1 and DNAJB6 are critical for regulation of polyglutamine aggregation. Scientific reports, 10(1), 1-9.

Jiang, B., Zhao, Y., Shi, M. O., Song, L., Wang, Q., Qin, Q., ... & Liu, X. (2020). DNAJB6 promotes ferroptosis in esophageal squamous cell carcinoma. Digestive diseases and sciences, 65(7), 1999-2008.

Zhang, L., Zhou, Q., Qiu, Q., Hou, L., Wu, M., Li, J., ... & Lu, Y. (2019). CircPLEKHM3 acts as a tumor suppressor through regulation of the miR-9/BRCA1/DNAJB6/KLF4/AKT1 axis in ovarian cancer. Molecular cancer, 18(1), 1-19.

Månsson, C., Van Cruchten, R. T., Weininger, U., Yang, X., Cukalevski, R., Arosio, P., ... & Emanuelsson, C. (2018). Conserved S/T residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation. Biochemistry, 57(32), 4891-4902.

Jonson, P. H., Palmio, J., Johari, M., Penttilä, S., Evilä, A., Nelson, I., ... & Udd, B. (2018). Novel mutations in DNAJB6 cause LGMD 1D and distal myopathy in French families. European Journal of Neurology, 25(5), 790-794.

Aprile, F. A., Källstig, E., Limorenko, G., Vendruscolo, M., Ron, D., & Hansen, C. (2017). The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation. Scientific reports, 7(1), 1-11.

Tsai, P. C., Tsai, Y. S., Soong, B. W., Huang, Y. H., Wu, H. T., Chen, Y. H., ... & Lee, Y. C. (2017). A novel DNAJB6 mutation causes dominantly inherited distal‐onset myopathy and compromises DNAJB6 function. Clinical Genetics, 92(2), 150-157.

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For research use only. Not intended for any clinical use.

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