E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation . Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress . Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction . Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1-mediated transcription of pro-apoptotic genes . Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes . Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3 . Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension . Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 . Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 . Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex . Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury . Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation . Mediates polyubiquitination of DNA polymerase beta at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome . Mediates polyubiquitination of CYP3A4 . Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation . Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation . Negatively regulates the suppressive function of regulatory T-cells during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner . Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome . Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity . Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation . Plays a role in the degradation of TP53 . Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation . May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation . Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis .

E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (Antigen NY-CO-7) (CLL-associated antigen KW-8) (Carboxy terminus of Hsp70-interacting protein) (RING-type E3 ubiquitin transferase CHIP) (STIP1 homology and U box-containing protein 1)

q9une7

Human, Mouse, Rat

WB,IF,ICC,IP

WB 1:2000-1:10000
IF 1:50-1:200
ICC 1:50-1:200
IP 1:20-1:50

~35 kD

Rabbit

50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Store at -20°C. Stable for 12 months from date of receipt.