Recombinant Human AMFR protein, His-tagged

• Cat.No.: AMFR-3763H
• Product Overview: Recombinant Human AMFR protein(301-643 aa), fused to His tag, was expressed in E. coli.

Specification

• Source: E. coli
• Species: Human
• Tag: His
• Form: The purified protein was Lyophilized from sterile PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH7.4). 5 % trehalose and 5 % mannitol are added as protectant before lyophilization. The elution buffer contain 300mM imidazole.
• Protein length: 301-643 aa
• AA Sequence: LFHEVQRRIRRHKNYLRVVGNMEAR FAVATPEELAVNNDDCAICWDSMQA ARKLPCGHLFHNSCLRSWLEQDTSC PTCRMSLNIADNNRVREEHQGENLD ENLVPVAAAEGRPRLNQHNHFFHFD GSRIASWLPSFSVEVMHTTNILGIT QASNSQLNAMAHQIQEMFPQVPYHL VLQDLQLTRSVEITTDNILEGRIQV PFPTQRSDSIRPALNSPVERPSSDQ EEGETSAQTERVPLDLSPRLEETLD FGEVEVEPSEVEDFEARGSRFSKSA DERQRMLVQRKDELLQQARKRFLNK SSEDDAASESFLPSEGASSDPVTLR RRMLAAAAERRLQKQQTS
• Purity: 90%, by SDS-PAGE with Coomassie Brilliant Blue staining.
• Storage: Short-term storage: Store at 2-8°C for (1-2 weeks).
  Long-term storage: Aliquot and store at -20°C to -80°C for up to 3 months, buffer containing 50% glycerol is recommended for reconstitution. Avoid repeat freeze-thaw cycles.
• Reconstitution: Reconstitute at 0.25 µg/μl in 200 μl sterile water for short-term storage.
  Reconstitution with 200 μl 50% glycerol solution is recommended for longer term storage.

Gene Information

• Gene Name: AMFR autocrine motility factor receptor, E3 ubiquitin protein ligase [ Homo sapiens ]
• Official Symbol: AMFR
• Synonyms: AMFR; autocrine motility factor receptor, E3 ubiquitin protein ligase; autocrine motility factor receptor; gp78; RNF45; RING finger protein 45; GP78
• Gene ID: 267
• mRNA Refseq: NM_001144
• Protein Refseq: NP_001135
• MIM: 603243
• UniProt ID: P26442

Reviews

10/04/2022

Accurate measurement of protein turnover rates.

09/28/2018

Reduced non-specific binding in antibody-based assays.

03/05/2017

Compatibility with high-resolution imaging techniques for detailed analysis.

Q&As

How does AMFR contribute to the regulation of protein turnover and degradation pathways, such as ubiquitin-proteasome system or autophagy?

AMFR 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.

What are the interacting partners of AMFR and their functional implications in protein quality control and degradation?

AMFR interacts with various cellular proteins involved in protein quality control, including chaperones, ubiquitin ligases, and components of the ERAD machinery.

What are the functional consequences of AMFR depletion or overexpression on cellular proteostasis and cell viability?

Depletion or overexpression of AMFR can disrupt cellular proteostasis, leading to the accumulation of misfolded proteins and impaired cell viability.

What is the role of AMFR in the clearance of misfolded or aggregated proteins, and how does it prevent their accumulation?

AMFR is responsible for recognizing and delivering misfolded or aggregated proteins for degradation, thereby preventing their accumulation and proteotoxicity.

What are the signaling pathways or post-translational modifications that regulate AMFR activity or stability?

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.

How does AMFR participate in the endoplasmic reticulum-associated degradation (ERAD) pathway?

AMFR participates in the endoplasmic reticulum-associated degradation (ERAD) pathway, which targets misfolded proteins in the ER for proteasomal degradation.

What is the cellular localization of AMFR protein and its subcellular distribution pattern?

AMFR protein is predominantly localized to the endoplasmic reticulum (ER), with a distribution pattern that includes ER membranes and ER-associated structures.

How does AMFR expression change under different cellular stress conditions, such as oxidative stress or ER stress?

AMFR expression can be upregulated in response to cellular stress, such as oxidative stress or endoplasmic reticulum (ER) stress.

Can targeting AMFR be a potential therapeutic approach for protein aggregation diseases or neurodegenerative disorders?

Targeting AMFR holds therapeutic potential for protein aggregation diseases and neurodegenerative disorders by promoting protein clearance and reducing protein aggregates' toxicity.

Can AMFR be involved in the regulation of cellular responses to DNA damage or genotoxic stress?

AMFR may have a role in coordinating cellular responses to DNA damage or genotoxic stress, potentially through its involvement in protein quality control mechanisms.