Recombinant Human E3 ubiquitin-protein ligase AMFR(AMFR),partial,Biotinylated CSB-EP892337HU1-B
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(Autocrine motility factor receptor)(AMF receptor)(RING finger protein 45)(gp78)
Species: (Organism)
Homo sapiens (Human)
Gene Names:
AMFR
Tag info:
N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged
Target Protein AA Sequence:
NSPVERPSSDQEEGETSAQTERVPLDLSPRLEETLDFGEVEVEPSEVEDFEARGSRFSKSADERQRMLVQRKDELLQQARKRFLNKS
Expression Region:
515-601aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
57.8 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
Function:
Involvement in disease:
Relevance:
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
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein." Shimizu K., Tani M., Watanabe H., Nagamachi Y., Niinaka Y., Shiroishi T., Ohwada S., Raz A., Yokota J. FEBS Lett. 456:295-300(1999).
