Analytical Data
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Gene name
HDAC6
- Application
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Alternative Names
HD6; JM21
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9UBN7
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Expression Region
Val166~Leu348
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Molecular Weight
22kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Histone deacetylase 6 (HDAC6) is a cytoplasmic enzyme that plays a crucial role in regulating various cellular processes, including protein degradation, cytoskeletal dynamics, and stress responses. Unlike classical HDACs that primarily target histones, HDAC6 uniquely deacetylates non-histone proteins, such as tubulin and heat shock protein 90 (HSP90), thereby influencing cell motility and apoptosis. Overexpression of HDAC6 has been linked to several pathological conditions, particularly cancer and neurodegenerative diseases, where its activity can promote tumor progression and neurotoxic responses. Given its significant involvement in these diseases, HDAC6 has emerged as a promising therapeutic target. Researchers are increasingly focused on the development of HDAC6 inhibitors, which may offer novel treatment strategies for conditions characterized by dysregulated acetylation. Exploring the structural and functional properties of recombinant HDAC6 proteins allows for a better understanding of its enzymatic mechanisms and interactions with substrates, which is essential for rational drug design. Additionally, the study of HDAC6's role in cellular signaling pathways has potential implications in the fields of regenerative medicine and immunology. As such, the comprehensive understanding of HDAC6 function and modulation can pave the way for innovative therapeutic interventions aimed at mitigating the impact of its dysregulation in various diseases.
