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Mouse Anti-HSPB8 Monoclonal Antibody (CBFYH-3252) (CBMAB-H0471-FY)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBFYH-3252
Antibody Isotype
IgG1, κ
Application
WB, IHC, IF, ELISA

Basic Information

Immunogen
His-tagged human recombinant HSP22
Specificity
Human, Mouse, Rat
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!]

Format
Liquid
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
Heat Shock Protein Family B (Small) Member 8
Introduction
The protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. The expression of this gene in induced by estrogen in estrogen receptor-positive breast cancer cells, and this protein also functions as a chaperone in association with Bag3, a stimulator of macroautophagy. Thus, this gene appears to be involved in regulation of cell proliferation, apoptosis, and carcinogenesis, and mutations in this gene have been associated with different neuromuscular diseases, including Charcot-Marie-Tooth disease.
Entrez Gene ID
Human26353
Mouse80888
Rat113906
UniProt ID
HumanQ9UJY1
MouseQ9JK92
RatQ9EPX0
Alternative Names
Heat Shock Protein Family B (Small) Member 8; Small Stress Protein-Like Protein HSP22; Heat Shock 27kDa Protein 8; Heat Shock 22kDa Protein 8; E2-Induced Gene 1 Protein; Alpha-Crystallin C Chain; Protein Kinase H11; E2IG1; HSP22;
Function
Displays temperature-dependent chaperone activity.
Biological Process
Cellular response to unfolded protein Source: ARUK-UCL
Positive regulation of aggrephagy Source: ARUK-UCL
Cellular Location
Cytoplasm; Nucleus. Translocates to nuclear foci during heat shock.
Involvement in disease
Neuronopathy, distal hereditary motor, 2A (HMN2A):
A neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.
Charcot-Marie-Tooth disease 2L (CMT2L):
An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
More Infomation

Chierichetti, M., Cerretani, M., Ciammaichella, A., Crippa, V., Rusmini, P., Ferrari, V., ... & Poletti, A. (2023). Identification of HSPB8 modulators counteracting misfolded protein accumulation in neurodegenerative diseases. Life Sciences, 322, 121323.

Cristofani, R., Piccolella, M., Crippa, V., Tedesco, B., Montagnani Marelli, M., Poletti, A., & Moretti, R. M. (2021). The role of HSPB8, a component of the chaperone-assisted selective autophagy machinery, in cancer. Cells, 10(2), 335.

Boczek, E. E., Fürsch, J., Niedermeier, M. L., Jawerth, L., Jahnel, M., Ruer-Gruß, M., ... & Stengel, F. (2021). HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain. Elife, 10, e69377.

Dubińska-Magiera, M., Niedbalska-Tarnowska, J., Migocka-Patrzałek, M., Posyniak, E., & Daczewska, M. (2020). Characterization of Hspb8 in zebrafish. Cells, 9(6), 1562.

Li, F., Yang, B., Li, T., Gong, X., Zhou, F., & Hu, Z. (2019). HSPB8 over‐expression prevents disruption of blood–brain barrier by promoting autophagic flux after cerebral ischemia/reperfusion injury. Journal of Neurochemistry, 148(1), 97-113.

Bouhy, D., Juneja, M., Katona, I., Holmgren, A., Asselbergh, B., De Winter, V., ... & Timmerman, V. (2018). A knock-in/knock-out mouse model of HSPB8-associated distal hereditary motor neuropathy and myopathy reveals toxic gain-of-function of mutant Hspb8. Acta neuropathologica, 135, 131-148.

Li, F., Xiao, H., Hu, Z., Zhou, F., & Yang, B. (2018). Exploring the multifaceted roles of heat shock protein B8 (HSPB8) in diseases. European Journal of Cell Biology, 97(3), 216-229.

Guilbert, S. M., Lambert, H., Rodrigue, M. A., Fuchs, M., Landry, J., & Lavoie, J. N. (2018). HSPB8 and BAG3 cooperate to promote spatial sequestration of ubiquitinated proteins and coordinate the cellular adaptive response to proteasome insufficiency. The FASEB Journal, 32(7), 3518-3535.

Cristofani, R., Crippa, V., Vezzoli, G., Rusmini, P., Galbiati, M., Cicardi, M. E., ... & Poletti, A. (2018). The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases. Cell Stress and Chaperones, 23, 1-12.

Li, F., Tan, J., Zhou, F., Hu, Z., & Yang, B. (2018). Heat shock protein B8 (HSPB8) reduces oxygen-glucose deprivation/reperfusion injury via the induction of mitophagy. Cellular Physiology and Biochemistry, 48(4), 1492-1504.

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

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