Biotinylated Recombinant Human E3 Ubiquitin-Protein Ligase Amfr (AMFR) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant Human E3 Ubiquitin-Protein Ligase Amfr (AMFR) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-00772P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Avi-tagged proteins, Biotinylated proteins, Featured biotinylated protein molecules, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human E3 Ubiquitin-Protein Ligase Amfr (AMFR) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UKV5
Target Symbol	AMFR
Synonyms	(Autocrine motility factor receptor)(AMF receptor)(RING finger protein 45)(gp78)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	NSPVERPSSDQEEGETSAQTERVPLDLSPRLEETLDFGEVEVEPSEVEDFEARGSRFSKSADERQRMLVQRKDELLQQARKRFLNKS
Expression Range	515-601aa
Protein Length	Partial
Mol. Weight	57.8 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins, such as CD3D, CYP3A4, CFTR, INSIG1, SOAT2/ACAT2 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-INSIG1 complex at the ER membrane. In addition, interaction of AMFR with AUP1 facilitates interaction of AMFR with ubiquitin-conjugating enzyme UBE2G2 and ubiquitin ligase RNF139, leading to sterol-induced HMGCR ubiquitination. The ubiquitinated HMGCR is then released from the ER into the cytosol for subsequent destruction. In addition to ubiquitination on lysine residues, catalyzes ubiquitination on cysteine residues: together with INSIG1, mediates polyubiquitination of SOAT2/ACAT2 at 'Cys-277', leading to its degradation when the lipid levels are low. Catalyzes ubiquitination and subsequent degradation of INSIG1 when cells are depleted of sterols. Mediates polyubiquitination of INSIG2 at 'Cys-215' in some tissues, leading to its degradation. Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex. 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. In association with LMBR1L and UBAC2, negatively regulates the canonical Wnt signaling pathway in the lymphocytes by promoting the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Database References	HGNC: 463 OMIM: 603243 KEGG: hsa:267 STRING: 9606.ENSP00000290649 UniGene: Hs.295137

Gene Functions References

There was a significant correlation between the 145 locus of the gp89 gene and coronary atherosclerotic heart disease, indexes of blood fat, blood glucose and blood pressure. PMID: 28212872
This is the first study to show that HSPA1L mediated HIF-1alpha stabilization. In addition, this is the first study to show that GP78 inactivation promotes cancer cell proliferation, migration and eventual tumor growth both in vivo and in vitro by increasing cellular prion protein. PMID: 28759037
overexpression of gp78 or SVIP suppression may eliminate the toxic gain of function associated with polymerization of ZAAT, thus providing a potential new therapeutic approach to the treatment of alpha-1 antitrypsin deficiency PMID: 28301499
Despite its interaction with gp78, Lnp does not seem to have a broad function in degradation of misfolded ER proteins. PMID: 27387505
Further study discovered that the gp78 CUE domain works as a proofreading machine during the growth of K48-linked polyubiquitin chains to ensure the linkage specificity. Together, our studies uncover a novel mechanism underlying the linkage specificity determination of longer polyubiquitin chains. PMID: 27067047
AMFR expression is significantly reduced in plasma from osteoporosis patients. PMID: 25689831
Catalytic inactivation of MGRN1 results in elevated levels of GP78 and a consequential increase in the initiation of mitophagy. PMID: 26743086
Authors conclude that the Hrd1 complex forms an essential retrotranslocation module that is evolutionarily conserved, but the mammalian ERAD system uses additional ubiquitin ligases to assist Hrd1 during retrotranslocation. PMID: 26424800
Downregulation of AMFR induced cell cycle arrest at the G0/G1 phase, and increased apoptosis of the THP1 cells. PMID: 26136223
The authors identify USP13 as a gp78-associated deubiquitinase that eliminates ubiquitin conjugates from Ubl4A to maintain the functionality of Bag6. PMID: 24424410
Data show that autocrine motility factor receptor (AMFR) and NOTCH1 protein are the direct target genes of microRNA miR-139-5p in colorectal cancer (CRC). PMID: 25149074
gp78 elongates polyubiquitin chains from the distal end through the cooperation of its G2BR and CUE domains. PMID: 25409783
Our data uncovers a previously unknown functional link between gp78 and TRIM25 and provides mechanistic insight into gp78-mediated protein ubiquitylation. PMID: 24810856
The ubiquitin ligase gp78, known for its role in protein quality control, is critical for unglycosylated PrP ubiquitylation and degradation. PMID: 24714645
High AMFR expression is associated with invasion depth and lymph node metastasis in gastric cancer. PMID: 24568530
DGAT2 is regulated by gp78-associated endoplasmic-reticulum-associated degradation at the post-translational level. PMID: 24820123
gp78 is expressed specifically in human prostate cancer rather than normal prostate tissues, it could be a putative biomarker for prostate cancer diagnosis. PMID: 23666464
data thus implicate two parallel pathways by which Gp78 regulates MAVS signaling PMID: 24285545
gp78 is a ubiquitination machine where multiple E2-binding sites coordinately facilitate processive ubiquitination. PMID: 23942235
A novel role for the endoplasmic reticulum-associated Gp78 ubiquitin ligase and the Mfn1 mitochondrial fusion factor in mitophagy. PMID: 23427266
The GP78 CUE domain functions to both facilitate substrate binding and enable switching between adjacent ubiquitin molecules of a growing chain to enable processivity in ubiquitination. PMID: 23123110
Delivery of ubiquitylated substrate to the central ER was regulated by ubiquitin chain elongation and opposing actions of gp78 CUE domain interactions and p97 recruitment. PMID: 22328510
This review summarizes the structure and function of GP78, and its importance in both physiological and pathological processes.[review] PMID: 22812524
cell surface expression of AMFR is associated with progression in Chronic lymphocytic leukemia PMID: 20574759
identify two ER membrane proteins, SPFH2 and TMUB1, as associated proteins of gp78, a membrane-bound ubiquitin ligase that mediates sterol-accelerated ERAD of the cholesterol biosynthetic enzyme HMG-CoA reductase. PMID: 21343306
AMFR pathway promotes invasion of esophageal squamous cell cancer cells PMID: 20504226
KAI1 has a role in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase PMID: 20089858
These data demonstrate a role of the E3 ubiquitin ligases in CTA1 retro-translocation. PMID: 19864457
The results support that gp78 is an E3 targeting CFTRDeltaF508 for degradation and Hrd1 inhibits CFTRDeltaF508 degradation by acting as an E3 for gp78. PMID: 19828134
Gp78 promotes SOD1 and ataxin-3 degradation in endoplasmic reticulum. PMID: 19661182
hippocampal expression of NLK and its receptor gp78 is associated with maze learning in rats. PMID: 11902125
In a prospective study we have also analyzed AMF receptor protein expression in primary tumors of 54 skin melanoma patients using IHC PMID: 12067203
demonstrate that GP78 is a bona fide E3 ligase in the apoB ER-associated degradation pathway PMID: 12670940
Autocrine motility factor receptor may contribute to tumor progression and AMF-R gene expression can serve as a useful prognostic marker in non-small cell lung cancers (NSCLC). PMID: 12962414
data provide evidence that the AMFR sequence coding for a seven-transmembrane domain E3 ubiquitin ligase codes for the gp78/AMFR protein recognized by the 3F3A mAb; the 3F3A mAb selectively recognizes a subpopulation of AMFR localized to an ER subdomain PMID: 15303277
Results identify gp78 as the E3 that initiates sterol-accelerated degradation of reductase, and Insig-1 as a bridge between gp78/VCP and the reductase substrate. PMID: 16168377
AMFR expression predicts an unfavourable surgical outcome in patients with stage I pulmonary adenocarcinomas PMID: 16184720
gp78-mediated ubiquitylation is an early step in endoplasmic reticulum -associated degradation PMID: 16407162
N-glyco side-chain of AMFR is a trigger and that interaction between the 117-C-terminal part of AMF and the extracellular core protein of AMFR is needed during AMF-AMFR interactions PMID: 16563432
These data indicate that gp78 assumes multiple unique quality control roles over ATZ, including the facilitation of degradation and inhibition of aggregation of ATZ. PMID: 16979136
Insig-1 sterol-regulated degradation is mediated by the membrane-bound ubiquitin ligase gp78 PMID: 17043353
the receptor molecule for AMF/NLK/MF in leukemic differentiation is not gp78 PMID: 17071500
Findings suggest a strong correlation between the expression of AMFR and RhoC and a correlation between them and invasion and metastasis of hepatocellular carcinoma. PMID: 17265125
Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube2g2 PMID: 17310145
This study identifies Ufd1 as a cofactor of gp78, reveals an unappreciated function of Ufd1 in the ubiquitination reaction during endoplasmic reticulum -associated degradation, and illustrates that Ufd1 plays a critical role in cholesterol metabolism. PMID: 17681147
SVIP is an endogenous inhibitor of ERAD that acts through regulating the assembly of the gp78-p97/VCP-Derlin1 complex. PMID: 17872946
gp78 promotes sarcoma metastasis by targeting KAI1 for degradation PMID: 18037895
both UBC7/gp78 and UbcH5a/CHIP may be involved in CYP3A4 ER-associated degradation, although their relative physiological contribution remains to be established PMID: 19103148
The G2BR domain within the E3 gp78 binds selectively and with high affinity to the E2 Ube2g2. PMID: 19560420
Hrd1 targets gp78 for proteasomal degradation independent of the ubiquitin ligase activity of gp78, without evidence of a reciprocal effect. PMID: 19835843

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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