Recombinant Human AMFR Protein, His-tagged

• Cat.No.: AMFR-514H
• Product Overview: Recombinant Human AMFR(Gln456~Ser643) fused with His tag at N-terminal was expressed in E. coli.

Specification

• Description: This locus encodes a glycosylated transmembrane receptor. Its ligand, autocrine motility factor, is a tumor motility-stimulating protein secreted by tumor cells. The encoded receptor is also a member of the E3 ubiquitin ligase family of proteins. It catalyzes ubiquitination and endoplasmic reticulum-associated degradation of specific proteins.
• Source: E. coli
• Species: Human
• Tag: His
• Form: PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
• Molecular Mass: 25.1kDa
• Protein length: Gln456~Ser643
• Endotoxin: <1.0EU per 1ug (determined by the LAL method)
• Purity: > 95%
• Applications: Positive Control; Immunogen; SDS-PAGE; WB.
  If bio-activity of the protein is needed, please check active protein
• Stability: The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 centigrade for 48h, and no obvious degradation and precipitation were observed. The loss rate is less than 5% within the expiration date under appropriate storage condition.
• Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 centigrade for one month. Aliquot and store at -80 centigrade for 12 months.
• Reconstitution: Reconstitute in PBS or others

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.