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HOP Rabbit mAb

Catalog No.: F4581

Application: Reactivity: Human, Monkey, Bovine

Usage Information

Dilution
WB1:1000 IF1:100 FCM1:50

Application
WB, IF, FCM

Reactivity
Human, Monkey, Bovine

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
64 kDa

Datasheet & SDS

Biological Description

Specificity
HOP Rabbit mAb recognizes endogenous levels of total HOP protein. This antibody is not known to cross-react with other heat shock proteins.

Clone
H14E22

Synonym(s)
Stress-induced-phosphoprotein 1, STI1, Hsc70/Hsp90-organizing protein (Hop), Renal carcinoma antigen NY-REN-11, Transformation-sensitive protein IEF SSP 3521, STIP1.

Background
HOP, also known as stress-induced phosphoprotein 1 (STIP1), is a co-chaperone that works with the major heat shock proteins Hsp70 and Hsp90, appearing in early receptor complexes. While it is predominantly located in the cytoplasm, it can also be found in the nucleus, associated with cell membranes, and in the extracellular environment. In mammals, HOP contains a bipartite nuclear localisation signal (NLS) that likely enables its movement from the cytoplasm to the nucleus in response to stress. It also has potential nuclear export signals, and blocking export increases its nuclear accumulation. The protein’s localisation is cell-cycle regulated: during the G1/S transition, casein kinase II-mediated phosphorylation promotes its nuclear translocation, whereas phosphorylation by cell division cycle 2 kinase retains it in the cytoplasm. Structurally, HOP is built from alternating tetratricopeptide repeat (TPR) motifs and aspartate-proline (DP) repeat domains. It contains three distinct TPR domains—TPR1, TPR2A, and TPR2B—each made up of three TPR motifs. These domains exhibit different binding preferences for Hsp70 and Hsp90. Mutations in TPR1 reduce Hsp70 interaction. By simultaneously binding both chaperones, HOP acts as an adaptor that bridges their functions. Although the roles of its two DP domains (DP1 and DP2) are not fully understood, HOP is an abundant and highly conserved protein crucial for coordinating chaperone networks.

Background

HOP, also known as stress-induced phosphoprotein 1 (STIP1), is a co-chaperone that works with the major heat shock proteins Hsp70 and Hsp90, appearing in early receptor complexes. While it is predominantly located in the cytoplasm, it can also be found in the nucleus, associated with cell membranes, and in the extracellular environment. In mammals, HOP contains a bipartite nuclear localisation signal (NLS) that likely enables its movement from the cytoplasm to the nucleus in response to stress. It also has potential nuclear export signals, and blocking export increases its nuclear accumulation. The protein’s localisation is cell-cycle regulated: during the G1/S transition, casein kinase II-mediated phosphorylation promotes its nuclear translocation, whereas phosphorylation by cell division cycle 2 kinase retains it in the cytoplasm. Structurally, HOP is built from alternating tetratricopeptide repeat (TPR) motifs and aspartate-proline (DP) repeat domains. It contains three distinct TPR domains—TPR1, TPR2A, and TPR2B—each made up of three TPR motifs. These domains exhibit different binding preferences for Hsp70 and Hsp90. Mutations in TPR1 reduce Hsp70 interaction. By simultaneously binding both chaperones, HOP acts as an adaptor that bridges their functions. Although the roles of its two DP domains (DP1 and DP2) are not fully understood, HOP is an abundant and highly conserved protein crucial for coordinating chaperone networks.

References
https://pubmed.ncbi.nlm.nih.gov/25487016/

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%