AAMP (Human) Recombinant Protein (Q01)
- Known as:
- AAMP (Human) Recombinant Protein (Q01)
- Catalog number:
- H00000014-Q01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- AAMP (Human) Recombinant Protein (Q01)
Related genes to: AAMP (Human) Recombinant Protein (Q01)
- Gene:
- AAMP NIH gene
- Name:
- angio associated migratory cell protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-13
- Date modifiied:
- 2016-10-04
Related products to: AAMP (Human) Recombinant Protein (Q01)
Related articles to: AAMP (Human) Recombinant Protein (Q01)
- The C-terminal to LisH (CTLH) complex is a modular multi-subunit E3 ligase with diverse biological functions, yet how its overall ubiquitylation activity is tuned remains unclear. Here, we identify CDK- and mTOR-dependent phosphorylation of the cognate E2 enzyme UBE2H as a key regulator of CTLH E3 catalytic capacity. Phosphorylation of two N-terminal serine residues (S3/S5) reduces UBE2H charging with ubiquitin, thereby limiting the pool of active E2 available to CTLH. Mitotic CDK activity inactivates UBE2H during mitosis, whereas mTOR restrains UBE2H charging in interphase to couple CTLH-dependent ubiquitylation to nutrient status. Preventing this phosphorylation maintains UBE2H charging, enhances CTLH-mediated substrate degradation, promotes CTLH subunit turnover, and causes proliferation and mitotic defects. Using hyperactive UBE2H, we identify two additional CTLH substrates, the mitotic kinase NEK9 and Angio-associated migratory cell protein (AAMP) and define a DR-like C-degron recognized by the CTLH subunit MKLN1. These findings reveal how regulation of an E2 enzyme by cell cycle and nutrient signaling pathways dynamically shape CTLH activity. - Source: PubMed
Publication date: 2026/03/09
Chen YingqianRossio ValentinaPaulo Joao AKarki MenukaManohar SandhyaOzimek NoelleFrizzi LauraGygi Steven PKing Randall W - Gallium-68 labeled peptide radiotracers have attracted significant attention in positron emission tomography (PET) imaging of various diseases. While Ga-DOTA radiolabeling protocols are well-established, two classes of peptides, disulfide-directed multicyclic peptides (DDMPs) and amphiphilic antimicrobial peptides (AAMPs), presented challenges in achieving satisfactory radiolabeling efficiency using existing methods. This study therefore aimed to establish optimized Ga-DOTA radiolabeling protocols specifically tailored to these peptides, in order to achieve high radiochemical purity (RCP) and radiochemical yield (RCY) suitable for clinical translation. By systematically varying key labeling conditions and purification methods such as pH, GaCl concentration, reaction time, purification cartridge and eluent types, and sterile filtration, two new radiolabeling protocols were developed for DDMP- and AAMP-based radiotracers. Detailed optimization identified an optimal pH of 3.6 combined with the use of concentrated GaCl for efficient radiolabeling of DDMPs, achieving RCY > 60% and RCP > 95%. For AAMPs, extended reaction time, hydrophilic-lipophilic balanced (HLB) cartridges, and ethanol/HCl elution improved RCY to > 60% with RCP > 90%. These results demonstrate that precise pH control and concentrated GaCl are essential for high labeling efficiency of DDMPs, whereas optimized purification methods are key for AAMPs. Importantly, this work provides efficient radiolabeling strategies for these two clinically promising classes of peptides and offers insights for optimizing labeling protocols for other peptides. The established methods will support subsequent Good Manufacturing Practice (GMP)-compliant manufacturing and facilitate the clinical translation of high-value radiopharmaceuticals with favorable in vivo performance. - Source: PubMed
Publication date: 2026/03/03
Chen XueyaoZhang SiqiJiang ShuoHu Kuan - Many E3 ubiquitin ligases recognize cognate degron motifs located at protein termini, but the paucity of substrates of N-degron and C-degron pathways hampers our understanding of their physiological significance. Here, by devising an expression screening approach to assess the effect of C-terminal "capping" on the stability of thousands of human proteins, we systematically identify a suite of full-length substrates harboring C-terminal degrons. Interrogating one leading candidate, ZMYND19, we characterize a C-degron pathway governed by the Muskelin substrate adaptor of the CTLH E3 ligase complex. Cell-to-cell variability in ZMYND19 stability uncovered conditional regulation, with CTLH-mediated degradation impaired by TNF-α stimulation but enhanced by mTOR inhibition. Parallel genetic and proteomic screens identified two poorly characterized proteins, AAMP and AEN, as additional substrates of the CTLH C-degron pathway, leading us to define an essential role for AAMP in ribosome maturation through chaperone activity towards ribosomal protein uL16. Altogether, these data define a C-degron pathway through which the Muskelin substrate adaptor connects conditional regulation of the CTLH E3 ligase complex to control of ribosome biogenesis. - Source: PubMed
Publication date: 2026/01/14
Grant Drew WTan ShengjiangRamage Dylan ELi Mamie ZDi YingTchasovnikarova Iva AWeekes Michael PElledge Stephen JWarren Alan JTimms Richard T - To investigate the clinical significance of abnormal expression of angio-associated migratory cell protein (AAMP) in hepatocellular carcinoma (HCC). - Source: PubMed
Li ChaoYin GuozhiCheng XiaoJiang Yezhen - To elucidate the oncogenic role of angio-associated migratory cell protein (AAMP) in colorectal cancer (CRC) and its mechanistic interplay with phosphoglycerate kinase 1 (PGK1). AAMP expression was analyzed in CRC and normal tissues (tissue microarrays-immunohistochemical/Western blot). Functional impacts were assessed via siRNA knockdown and lentiviral overexpression in CRC cell lines (proliferation: CCK-8/3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide/clonogenic assays; tumorigenesis: xenografts). Molecular mechanisms were explored through co-immunoprecipitation, phosphorylation assays, and Ribonucleic Acid (RNA) sequencing. AAMP was significantly upregulated in CRC versus normal tissues ( < 0.05), correlating with poor patient survival. AAMP knockdown suppressed CRC cell proliferation, colony formation, and xenograft tumor growth, whereas overexpression exacerbated these phenotypes. Mechanistically, AAMP directly bound PGK1 and enhanced its phosphorylation (p-PGK1), driving CRC proliferation. PGK1 silencing abrogated AAMP-mediated proliferative effects. RNA sequencing revealed AAMP modulation of immune-related pathways (Tumor Necrosis Factor, IL-17, Jak-STAT) and key proteins (EGFR, RPL10, NOD2), suggesting dual roles in proliferation. AAMP promotes CRC progression through PGK1 phosphorylation-dependent metabolic activation, proposing the AAMP-PGK1 axis as a therapeutic target for advanced CRC. - Source: PubMed
Publication date: 2025/06/16
Zhang WeiShi QianLiu QinchengZhang HaomiaoXia JiZhang Xueli