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Anti-Hsp105/HSP110 Rabbit Antibody [G11F18]

Catalog No.: F3718

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 - 1:10000 IP1:1000 - 1:10000 IHC1:50 - 1:500 IF1:100 - 1:250

Application
WB, IP, IHC, IF

Reactivity
Mouse, Rat, Human

Source
Rabbit

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
97 kDa 105 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human liver carcinoma tissue; Human thyroid gland carcinoma tissue; Human cerebellum; HeLa; HepG2; C6; PC-12; NIH/3T3; MCF-7
Negative Control

Datasheet & SDS

Biological Description

Specificity
Hsp105/HSP110 Rabbit mAb detects endogenous levels of total Hsp105/HSP110 protein.

Clone
G11F18

Synonym(s)
HSP105, HSP110, KIAA0201, HSPH1, Heat shock protein 105 kDa, Antigen NY-CO-25, Heat shock 110 kDa protein, Heat shock protein family H member 1

Background
Hsp105/HSP110 is a molecular chaperone belonging to the Hsp70 superfamily, distinguished by its dual function as a nucleotide exchange factor (NEF) for Hsp70 chaperones and as an independent ATP-dependent "holdase" chaperone that prevents protein aggregation during cellular stress. It consists of two main domains: an N-terminal nucleotide-binding domain (NBD) responsible for ATP binding and hydrolysis, critical for energy transduction, and a C-terminal substrate-binding domain (SBD) that recognizes and stabilizes unfolded or misfolded polypeptides. Unique structural features, such as an extended loop region and conserved helix-rich motifs, facilitate these substrate and co-chaperone interactions. Hsp105/HSP110 collaborates with Hsp70 and Hsp40 cochaperones to form a potent triad that catalyzes the disaggregation and refolding of stable misfolded proteins, efficiently converting aggregates to native conformations. Hsp105/HSP110 alone also exhibits bona fide chaperone activity, utilizing ATP hydrolysis to unfold misfolded substrates, underscoring its active role beyond nucleotide exchange. This chaperone machinery is pivotal in maintaining proteostasis under normal and stress conditions, regulating the folding and quality control of aggregation-prone proteins, including membrane proteins such as the cystic fibrosis transmembrane conductance regulator (CFTR) and its ΔF508 mutant implicated in cystic fibrosis. Dysregulation or altered expression of Hsp105/HSP110 is linked to diseases involving protein misfolding, such as cystic fibrosis and cancer.

Background

Hsp105/HSP110 is a molecular chaperone belonging to the Hsp70 superfamily, distinguished by its dual function as a nucleotide exchange factor (NEF) for Hsp70 chaperones and as an independent ATP-dependent "holdase" chaperone that prevents protein aggregation during cellular stress. It consists of two main domains: an N-terminal nucleotide-binding domain (NBD) responsible for ATP binding and hydrolysis, critical for energy transduction, and a C-terminal substrate-binding domain (SBD) that recognizes and stabilizes unfolded or misfolded polypeptides. Unique structural features, such as an extended loop region and conserved helix-rich motifs, facilitate these substrate and co-chaperone interactions. Hsp105/HSP110 collaborates with Hsp70 and Hsp40 cochaperones to form a potent triad that catalyzes the disaggregation and refolding of stable misfolded proteins, efficiently converting aggregates to native conformations. Hsp105/HSP110 alone also exhibits bona fide chaperone activity, utilizing ATP hydrolysis to unfold misfolded substrates, underscoring its active role beyond nucleotide exchange. This chaperone machinery is pivotal in maintaining proteostasis under normal and stress conditions, regulating the folding and quality control of aggregation-prone proteins, including membrane proteins such as the cystic fibrosis transmembrane conductance regulator (CFTR) and its ΔF508 mutant implicated in cystic fibrosis. Dysregulation or altered expression of Hsp105/HSP110 is linked to diseases involving protein misfolding, such as cystic fibrosis and cancer.

References
https://pubmed.ncbi.nlm.nih.gov/23737532/ https://pubmed.ncbi.nlm.nih.gov/22505710/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%