Product Description
VDU1 Antibody | 61-123 | ProSci
Host: Rabbit
Reactivity: Human
Homology: Predicted species reactivity based on immunogen sequence: Bovine
Immunogen: This VDU1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 799-829 amino acids from the C-terminal region of human VDU1.
Research Area: Cell Cycle
Tested Application: WB
Application: For WB starting dilution is: 1:1000
Specificiy: N/A
Positive Control 1: N/A
Positive Control 2: N/A
Positive Control 3: N/A
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: 107 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: Ubiquitin carboxyl-terminal hydrolase 33, Deubiquitinating enzyme 33, Ubiquitin thioesterase 33, Ubiquitin-specific-processing protease 33, VHL-interacting deubiquitinating enzyme 1, hVDU1, USP33, KIAA1097, VDU1
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: Type 2 iodothyronine deiodinase (D2) is an integral membrane selenoenzyme that stimulates the pro-hormone thyroxine (T4) and supplies the majority of the 3, 5, 3?-triiodothyronine (T3) essential for brain development.1 T4 catalysis accelerates selective conjugation to ubiquitin and thereby renders D2 inactive, a posttranslational feedback mechanism used to maintain acceptable T3 levels.2, 3 Ub-D2 was the first recognized substrate for von Hippel?Lindau protein?interacting (pVHL-interacting) deubiquitinating enzyme-1 (VDU1) .4 VDU proteins colocalize with D2 in the endoplasmic reticulum, and their coexpression provides D2 resistance to degradation. VDU1 expression is substantially upregulated in brown adipocytes by norepinephrine or cold exposure, further amplifying D2 activity. VDU1 and VDU2 are coexpressed with D2 in many human tissues, including brain, heart, and skeletal muscle, suggesting potential roles in neurological development, cardiac function, and energy management, in addition to thermal homeostasis.VDU1- or VDU2-catalyzed deubiquitination recycles inactive Ub-D2 to its active deubiquitinated form, circumventing the proteasomal degradation pathway. Thus, Ub-D2 can be either reactivated or degraded, with the balance between these two processes influenced by VDU activity.VDU1-catalyzed D2 deubiquitination may be an important participant in the adaptive mechanism that regulates thyroid hormone action. The reversible ubiquitination-dependent mechanism regulating D2 activity permits highly responsive control of thyroid hormone activation.5, 6