Recombinant Human HECT domain-containing 2 Protein, CF
Recombinant Human HECT domain-containing 2 Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||X mg/ml (X μM) in 50 mM HEPES, pH 7.0, 100 mM NaCl, 5% (v/v) Glycerol, 5 mM DTT|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
HECTD2 (aka "HECT domain-containing protein 2" or "HECT-type E3 ubiquitin transferase HECTD2") is a 776 amino acid member of the HECT (Homologous to E6AP Carboxyl Terminus) domain family of Ubiquitin ligases. With a predicted weight of 88 kDa, human HECTD2 shares 89% identity and 94% similarity with the mouse orthologue. In innate immunity HECTD2 exerts a pro-inflammatory effect by contributing to the ubiquitylation and degradation of PIAS1, a multifunctional and potent anti-inflammatory protein that negatively regulates several key inflammatory pathways. Small molecule inhibitors of HECTD2 were found to attenuate lipopolysaccharide (LPS)-induced lung inflammation. HECTD2 has also been shown to ubiquitylate BoNT/A, a catalytic light chain of botulinum neurotoxin. Ubiquitylation can lead to the proteasomal degradation of the light chain, but it's rescued from destruction by the dominant effect of a deubiquitinating enzyme, VCIP135/VCPIP1.
- Coon T.A. et al. (2015) Sci. Transl. Med. doi: 10.1126/scitranslmed.aab3881
- Tsai Y.C. et al. (2017) Proc. Natl. Acad. Sci. 114: E5158-E5166
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