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Mouse Anti-HSPB6 Recombinant Antibody (6A4) (CBMAB-A4133-LY)

The product is antibody recognizes HSPB6. The antibody 6A4 immunoassay techniques such as: WB, ELISA.
See all HSPB6 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
6A4
Antibody Isotype
IgG2a, λ
Application
WB, ELISA

Basic Information

Immunogen
HSPB6 (AAH68046.1, 1 a.a. ~ 160 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, λ
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
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Heat Shock Protein Family B (Small) Member 6
Introduction
HSPB6 is associated with actin (see MIM 102540) and modulates smooth muscle relaxation (Tessier et al., 2003 [PubMed 12842460]).[supplied by OMIM
Entrez Gene ID
126393
UniProt ID
O14558
Alternative Names
FLJ32389; Hsp20
Function
Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.
Biological Process
Chaperone-mediated protein folding Source: UniProtKB
Positive regulation of angiogenesis Source: UniProtKB
Cellular Location
Nucleus; Secreted; Cytoplasm. Translocates to nuclear foci during heat shock.
PTM
The N-terminus is blocked.
Phosphorylated at Ser-16 by PKA and probably PKD1K; required to protect cardiomyocytes from apoptosis.

Almutairi, B. O., Almutairi, M. H., Alrefaei, A. F., Alkahtani, S., & Alarifi, S. (2023). HSPB6 Is Depleted in Colon Cancer Patients and Its Expression Is Induced by 5-aza-2′-Deoxycytidine In Vitro. Medicina, 59(5), 996.

Pfeffer, T. J., Auber, B., Pabst, B., Agca, K. C., Berliner, D., König, T., ... & Ricke-Hoch, M. (2023). Prevalence of HSPB6 gene variants in peripartum cardiomyopathy: Data from the German PPCM registry. International Journal of Cardiology, 379, 96-99.

Kumar, R., Gupta, I. D., Verma, A., Singh, S., Kumari, R., & Verma, N. (2022). Genetic polymorphism in HSPB6 gene and their association with heat tolerance traits in Indian Karan Fries (Bos taurus x Bos indicus) cattle. Animal Biotechnology, 33(7), 1416-1427.

Shatov, V. M., & Gusev, N. B. (2020). Physico-chemical properties of two point mutants of small heat shock protein HspB6 (Hsp20) with abrogated cardioprotection. Biochimie, 174, 126-135.

Mikhaylova, V. V., Eronina, T. B., Chebotareva, N. A., Shubin, V. V., Kalacheva, D. I., & Kurganov, B. I. (2020). Effect of arginine on chaperone-like activity of HspB6 and monomeric 14-3-3ζ. International journal of molecular sciences, 21(6), 2039.

Qi, A. Q., Zhang, Y. H., Qi, Q. D., Liu, Y. H., & Zhu, J. L. (2019). Overexpressed HspB6 underlines a novel inhibitory role in kainic acid-induced epileptic seizure in rats by activating the cAMP-PKA pathway. Cellular and Molecular Neurobiology, 39, 111-122.

Shatov, V. M., Weeks, S. D., Strelkov, S. V., & Gusev, N. B. (2018). The role of the arginine in the conserved N-terminal domain RLFDQxFG motif of human small heat shock proteins HspB1, HspB4, HspB5, HspB6, and HspB8. International Journal of Molecular Sciences, 19(7), 2112.

Liu, G. S., Zhu, H., Cai, W. F., Wang, X., Jiang, M., Essandoh, K., ... & Kranias, E. G. (2018). Regulation of BECN1-mediated autophagy by HSPB6: Insights from a human HSPB6S10F mutant. Autophagy, 14(1), 80-97.

Li, F., Xiao, H., Zhou, F., Hu, Z., & Yang, B. (2018). Study of HSPB6: insights into the properties of the multifunctional protective agent. Cellular Physiology and Biochemistry, 44(1), 314-332.

Ferreira, L. A., Gusev, N. B., Uversky, V. N., & Zaslavsky, B. Y. (2018). Effect of human heat shock protein HspB6 on the solvent features of water in aqueous solutions. Journal of Biomolecular Structure and Dynamics, 36(6), 1520-1528.

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

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