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AMFR Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
United StatesOrdering Information
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|Catalog #||Size||Availability||Available Date|
(40 western blots)
|Backorder||4 months||DISCONTINUED INQUIRE CLICK Add to cart|
(8 western blots)
|Backorder||4 months||DISCONTINED INQUIRE CLICK Add to cart|
- Citations : 1
AMFR Antibody (N-term) - Product info
|Application ||WB, IHC, FC|
|Calculated MW||72996 Da|
AMFR Antibody (N-term) - Additional info
|Gene ID 267|
AMFR; RNF45; E3 ubiquitin-protein ligase AMFR; Autocrine motility factor receptor, isoform 2; RING finger protein 45; gp78
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.
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.
Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
AMFR Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
AMFR Antibody (N-term) - Protein Information
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.
Endoplasmic reticulum membrane; Multi-pass membrane protein
AMFR Antibody (N-term) - Related products
AMFR Antibody (N-term) - Research Areas
Western blot analysis of AMFR (arrow) using AMFR Antibody (N-term) (Cat.#AP2162a). 293 cell lysates (2 ug/lane) either nontransfected (Lane 1) or transiently transfected with the AMFR gene (Lane 2) (Origene Technologies).
Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
Formalin-fixed and paraffin-embedded human hepatocarcinoma tissue reacted with AMFR Antibody (N-term) (Cat.#AP2162a), which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.
Flow cytometric analysis of HepG2 cells using AMFR Antibody (N-term)(bottom histogram) compared to a negative control cell (top histogram). FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.
Phosphoglucose isomerase/autocrine motility factor promotes melanoma cell migration through ERK activation dependent on autocrine production of interleukin-8.
Author : Araki K, Shimura T, Yajima T, Tsutsumi S, Suzuki H, Okada K, Kobayashi T, Raz A, Kuwano H.
J Biol Chem. 2009 Nov 20;284(47):32305-11. doi: 10.1074/jbc.M109.008250. Epub 2009 Sep 30.
PubMed® Id : 19801670
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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).