- CITATIONS: 1
|Application ||WB, IHC-P, FC, E|
|Calculated MW||72996 Da|
|Antigen Region||571-601 aa|
|Other Names||E3 ubiquitin-protein ligase AMFR, 632-, Autocrine motility factor receptor, AMF receptor, RING finger protein 45, gp78, AMFR, RNF45|
|Target/Specificity||This AMFR antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 571-601 amino acids from the N-terminal region of human AMFR.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|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||AMFR Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97- AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97- AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor.|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
Provided below are standard protocols that you may find useful for product applications.
Autocrine motility factor (AMF) is a protein secreted by tumor cells that stimulates tumor motility. The gene for AMFR encodes a 323-amino acid polypeptide that has a single transmembrane domain and several putative glycosylation sites. The protein sequence has some homology to human tumor protein p53.
Huang, B., et al., Biochem. Biophys. Res. Commun. 212(3):727-742 (1995).
Watanabe, H., et al., J. Biol. Chem. 266(20):13442-13448 (1991).
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