AMFR
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Official Full Name
autocrine motility factor receptor, E3 ubiquitin protein ligase
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Overview
Autocrine motility factor receptor (AMFR/gp78) is a putative seven transmembrane domain G protein-coupled receptor that functions, in part, at the cell surface as a cytokine receptor for autocrine motility factor/phosphoglucose isomerase (AMF/PGI). AMFR i -
Synonyms
AMFR; autocrine motility factor receptor, E3 ubiquitin protein ligase; autocrine motility factor receptor; gp78; RNF45; RING finger protein 45;
- Recombinant Proteins
- Homo sapiens (Human)
- Human
- Mouse
- Mus musculus (Mouse)
- Zebrafish
- E.coli
- E.coli expression system
- E.Coli or Yeast
- In vitro E. coli expression system
- Mammalian Cell
- Wheat Germ
- GST
- His
| Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| Human | AMFR-3783H | Recombinant Human AMFR, GST-tagged | E.Coli or Yeast | GST | 643 |
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| Human | AMFR-520H | Recombinant Human AMFR protein, GST-tagged | Wheat Germ | GST |
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| Human | AMFR-514H | Recombinant Human AMFR Protein, His-tagged | E.coli | His | Gln456~Ser643 |
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| Human | AMFR-204H | Recombinant Human AMFR Full Length Transmembrane protein, His-tagged | In vitro E. coli expression system | His | 1-643aa |
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| Human | AMFR-3763H | Recombinant Human AMFR protein, His-tagged | E.coli | His | 301-643 aa | |
| Mouse | Amfr-515M | Recombinant Mouse Amfr Protein, His-tagged | E.coli | His | Met456~Thr639 |
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| Homo sapiens (Human) | RFL22538HF | Recombinant Full Length Human E3 Ubiquitin-Protein Ligase Amfr(Amfr) Protein, His-Tagged | E.coli expression system | His | Full Length (1-643) |
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| Mus musculus (Mouse) | RFL32124MF | Recombinant Full Length Mouse E3 Ubiquitin-Protein Ligase Amfr(Amfr) Protein, His-Tagged | E.coli expression system | His | Full Length (1-643) |
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| Zebrafish | AMFR-12379Z | Recombinant Zebrafish AMFR | Mammalian Cell | His |
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- Involved Pathway
- Protein Function
- Interacting Protein
- AMFR Related Articles
- AMFR Related Research Area
AMFR involved in several pathways and played different roles in them. We selected most pathways AMFR participated on our site, such as Protein processing in endoplasmic reticulum, which may be useful for your reference. Also, other proteins which involved in the same pathway with AMFR were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Protein processing in endoplasmic reticulum | ERO1LB;STT3A;CRYAB;DNAJC5GB;MOGS;PRKCSH;UBQLN1;NSFL1C;CCDC102A |
AMFR has several biochemical functions, for example, BAT3 complex binding, chaperone binding, ligase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by AMFR itself. We selected most functions AMFR had, and list some proteins which have the same functions with AMFR. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| BAT3 complex binding | USP13;SGTA;VCP;AMFR |
| chaperone binding | AHSA1L;CDC37L1;DNAJB2;TIMM44;HES1;CP;H2-KE2;DLST;AMFR |
| ligase activity | TRIML2;MIB2;ITCH;PRP19;MGRN1;RLIM;UBE2KA;TRIM21;SYVN1 |
| protein binding | C10orf33;KCNMA1;CCDC123;WDTC1;TGFBI;ADCK5;BCL2;IFI6;TNIP1 |
| protein binding, bridging | SYNM;ANK2;CNKSR1;WWC1;AMFR;CUX1;RAD50;FRMD4A;FKBP4 |
| receptor activity | DERL1;NOTCH1;KLRK1;ICAM1;TNFRSF11B;TNFRSF9;RAMP3;PVRL1A;CLEC4E |
| ubiquitin protein ligase activity | HUWE1;MED1;FANCF;MED7;RNF24;PELI1;PDZRN3;MYLIP;UBE2G1 |
| ubiquitin protein ligase activity involved in ERAD pathway | RNF5;TMEM129;STUB1;AMFR;RNF185;SYVN1;PARK2;TRIM25 |
| ubiquitin-protein transferase activity | MARCH5;TRIP12;RNF13;RNF181;RNF5;UBE2B;MIB2;UBE2Q2;RNF38 |
| ubiquitin-specific protease binding | PARK2;SART3;MARCH6;BAG6;DERL1;CHMP3;AMFR;VPS24;RAD23A |
| ubiquitin-ubiquitin ligase activity | PRPF19;UBOX5;UBE2K;UBE4B;RBX1;PPIL2;STUB1;AMFR;ANAPC11 |
| zinc ion binding | TRIM15;RNF133;CA15C;TRIM46B;AGBL1;GATA5;SH3RF3;UMPS;CA13 |
AMFR has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AMFR here. Most of them are supplied by our site. Hope this information will be useful for your research of AMFR.
UBE2G2; VCP
- Q&As
- Reviews
Q&As (10)
Ask a questionAMFR plays a crucial role in protein turnover and degradation pathways, promoting the degradation of misfolded or unwanted proteins through the ubiquitin-proteasome system and autophagy.
AMFR interacts with various cellular proteins involved in protein quality control, including chaperones, ubiquitin ligases, and components of the ERAD machinery.
Depletion or overexpression of AMFR can disrupt cellular proteostasis, leading to the accumulation of misfolded proteins and impaired cell viability.
AMFR is responsible for recognizing and delivering misfolded or aggregated proteins for degradation, thereby preventing their accumulation and proteotoxicity.
AMFR activity and stability can be regulated by post-translational modifications, such as ubiquitination or phosphorylation, and by signaling pathways, including the unfolded protein response (UPR) pathway.
AMFR participates in the endoplasmic reticulum-associated degradation (ERAD) pathway, which targets misfolded proteins in the ER for proteasomal degradation.
AMFR protein is predominantly localized to the endoplasmic reticulum (ER), with a distribution pattern that includes ER membranes and ER-associated structures.
AMFR expression can be upregulated in response to cellular stress, such as oxidative stress or endoplasmic reticulum (ER) stress.
Targeting AMFR holds therapeutic potential for protein aggregation diseases and neurodegenerative disorders by promoting protein clearance and reducing protein aggregates' toxicity.
AMFR may have a role in coordinating cellular responses to DNA damage or genotoxic stress, potentially through its involvement in protein quality control mechanisms.
Customer Reviews (3)
Write a reviewAccurate measurement of protein turnover rates.
Reduced non-specific binding in antibody-based assays.
Compatibility with high-resolution imaging techniques for detailed analysis.
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