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Rabbit Anti-STUB1 Polyclonal Antibody#abs135823

Description

Catalog-specification	Delivery time	USD price
abs135823-100ug	1-2 Weeks	301.0
abs135823-50ug	1-2 Weeks	201.0

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Overview
catalog	abs135823
Description	CHIP, also known as STUB1, is a co-chaperone protein that acts as a functional E3 ubiquitin ligase. Its role is to connect the polypeptide binding activity of Hsp70 to the ubiquitin proteasome system. The cytoplasmic form of CHIP contains three TPR domains at its amino terminus, each consisting of 34 amino acids, and a U-box domain at its carboxy terminus. The TPR domains allow CHIP to interact with molecular chaperones Hsc70-Hsp70 and Hsp90, while the U-box domain is responsible for its E3 ubiquitin ligase activity. Binding of CHIP to Hsp70 can inhibit the folding process of Hsp70 client proteins and promote the U-box dependent ubiquitination of substrates bound to Hsp70. CHIP plays a crucial role in cellular stress response and is involved in the degradation of various disease-related proteins, including cystic fibrosis transmembrane conductance regulator, p53, huntingtin and Ataxin-3, Tau protein, and α-synuclein.
Other names	The Antigen NY CO-7, also known as Carboxy terminus of Hsp70-interacting protein or CHIP, is an E3 ubiquitin protein ligase. It interacts with Hsp70 and is involved in the degradation of damaged or misfolded proteins. It is also associated with CLL, colon cancer, and is expressed in various tissues. Additionally, it contains a U-Box domain similar to a component of the endoplasmic reticulum degradation pathway. With its STIP1 homology and U-box containing protein 1, CHIP plays an essential role in the ubiquitin-proteasome system. Hence, variations in CHIP expression levels and functionality could have significant implications for protein quality control and cellular homeostasis.
Source	Rabbit
Specificity	The STUB1 Antibody is capable of detecting total STUB1 at endogenous levels. This information can be restated by saying that the antibody is capable of identifying the overall amount of STUB1 present in a sample at levels that are naturally occurring within the sample.
Species Reactivity	Human;Mouse;Rat;Monkey
Predictive reaction species	Xenopus;Chicken;Sheep;Dog;Bovine;Horse;
Antigen	STUB1
Application	WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
Immunogen	A synthesized peptide derived from human STUB1.
MW	35kDa
Properties
Concentration	1mg/ml
purification	The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin .
Clonality	Polyclonal Antibody
Stability & Storage	Store at -20 °C for one year. Avoid repeated freeze/thaw cycles
Storage buffer	Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
Target
Background	E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. 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. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) 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 (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385).
Tissue specificity	Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung.
Posttranslational modification	Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 (By similarity). Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2.
Celluar localization	Cytosol;Endoplasmic reticulum;Extracellular region or secreted;Nucleus;
UniPort	Q9UNE7