EHD1 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q9H4M9 |
Other Accession | Q641Z6, Q9WVK4, Q5E9R3, NP_006786.2 |
Reactivity | Human |
Predicted | Bovine, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 60627 Da |
Antigen Region | 410-438 aa |
Gene ID | 10938 |
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Other Names | EH domain-containing protein 1, PAST homolog 1, hPAST1, Testilin, EHD1, PAST, PAST1 |
Target/Specificity | This EHD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 410-438 amino acids from the C-terminal region of human EHD1. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | EHD1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | EHD1 (HGNC:3242) |
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Function | ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes (PubMed:24019528). Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (By similarity). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (By similarity). Plays a role in the formation of the ciliary vesicle (CV), an early step in cilium biogenesis. Proposed to be required for the fusion of distal appendage vesicles (DAVs) to form the CV by recruiting SNARE complex component SNAP29. Is required for recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization before Rab8-dependent ciliary membrane extension. Required for the loss of CCP110 form the mother centriole essential for the maturation of the basal body during ciliogenesis (PubMed:25686250). |
Cellular Location | Recycling endosome membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:Q9WVK4}; Peripheral membrane protein; Cytoplasmic side. Cell projection, cilium membrane; Peripheral membrane protein; Cytoplasmic side. Note=Preferentially associates with tubular recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:19864458, PubMed:23596323). Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes (By similarity) Localizes to the ciliary pocket from where the cilium protrudes (PubMed:25686250). Colocalizes with BACE1 in tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta proteins in hippocampal mossy fiber terminals (By similarity) {ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:23596323, ECO:0000269|PubMed:25686250} |
Tissue Location | Highly expressed in testis. |
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Background
This gene belongs to a highly conserved gene family encoding EPS15 homology (EH) domain-containing proteins. The protein-binding EH domain was first noted in EPS15, a substrate for the epidermal growth factor receptor. The EH domain has been shown to be an important motif in proteins involved in protein-protein interactions and in intracellular sorting. The protein encoded by this gene is thought to play a role in the endocytosis of IGF1 receptors.
References
Gudmundsson, H., et al. Circ. Res. 107(1):84-95(2010)
Sharma, M., et al. Mol. Biol. Cell 20(24):5181-5194(2009)
Kieken, F., et al. Protein Sci. 18(12):2471-2479(2009)
Jovic, M., et al. Mol. Biol. Cell 20(11):2731-2743(2009)
Fichtman, B., et al. Cell. Mol. Biol. Lett. 13(4):632-648(2008)
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