AntiHuman IL 1 Alpha (C42) Purified
- Known as:
- AntiHuman Interleukin 1 Alpha (C42) Purified
- Catalog number:
- irag132-0.2mg
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Innovative research
- Gene target:
- AntiHuman 1 Alpha (C42) Purified
Related genes to: AntiHuman IL 1 Alpha (C42) Purified
- Gene:
- AMMECR1L NIH gene
- Name:
- AMMECR1 like
- Previous symbol:
- -
- Synonyms:
- MGC4268
- Chromosome:
- 2q14.3
- Locus Type:
- gene with protein product
- Date approved:
- 2007-01-26
- Date modifiied:
- 2016-10-05
- Gene:
- ARHGAP1 NIH gene
- Name:
- Rho GTPase activating protein 1
- Previous symbol:
- -
- Synonyms:
- RhoGAP, p50rhoGAP, CDC42GAP, Cdc42GAP
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2014-11-18
- Gene:
- CCDC42 NIH gene
- Name:
- coiled-coil domain containing 42
- Previous symbol:
- -
- Synonyms:
- FLJ32734, CCDC42A
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-12-15
- Date modifiied:
- 2015-10-06
- Gene:
- CDC42 NIH gene
- Name:
- cell division cycle 42
- Previous symbol:
- -
- Synonyms:
- G25K, CDC42Hs
- Chromosome:
- 1p36.12
- Locus Type:
- gene with protein product
- Date approved:
- 1991-06-06
- Date modifiied:
- 2019-04-23
- Gene:
- CDK5RAP1 NIH gene
- Name:
- CDK5 regulatory subunit associated protein 1
- Previous symbol:
- C20orf34
- Synonyms:
- CGI-05, HSPC167, C42
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-21
- Date modifiied:
- 2014-11-19
Related products to: AntiHuman IL 1 Alpha (C42) Purified
Related articles to: AntiHuman IL 1 Alpha (C42) Purified
- - Source: PubMed
Publication date: 2024/05/02
Sanesteban-Beceiro EstebanFenollar-Cortés MaríaHerrero-Forte ClaraGómez-Mayordomo VictorCatalán-Alonso María JAlonso-Frech Fernando - The gene encodes the α-subunit of mitochondrial processing peptidase (α-MPP), an enzyme responsible for cleavage of nuclear-encoded mitochondrial precursor proteins after their import into mitochondria. Mutations in this gene have been described in patients with nonprogressive or slow progressive cerebellar ataxia, with variable age at onset and severity. Cerebellar atrophy and striatum changes were found in severe cases. - Source: PubMed
Publication date: 2023/11/14
Rambani VibhutiKolnikova MiriamCagalinec MichalSkopkova MartinaGasperikova Daniela - To explore the differences in the cortical morphometric similarity network (MSN) between COVID-19 survivors and healthy controls, and the correlation between these differences and behavioralfeatures and transcriptional signatures. - Source: PubMed
Publication date: 2023/08/23
Long JiaLi JiaoXie BingJiao ZhuominShen GuoqiangLiao WeiSong XiaominLe HongboXia JunWu Song - HtrA2/Omi is a mitochondrial serine protease with ascribed pro-apoptotic as well as pro-necroptotic functions. Here, we establish that HtrA2/Omi also controls parthanatos, a third modality of regulated cell death. Deletion of HtrA2/Omi protects cells from parthanatos while reconstitution with the protease restores the parthanatic death response. The effects of HtrA2/Omi on parthanatos are specific and cannot be recapitulated by manipulating other mitochondrial proteases such as PARL, LONP1 or PMPCA. HtrA2/Omi controls parthanatos in a manner mechanistically distinct from its action in apoptosis or necroptosis, i.e., not by cleaving cytosolic IAP proteins but rather exerting its effects without exiting mitochondria, and downstream of PARP-1, the first component of the parthanatic signaling cascade. Also, previously identified or candidate substrates of HtrA2/Omi such as PDXDC1, VPS4B or moesin are not cleaved and dispensable for parthanatos, whereas DBC-1 and stathmin are cleaved, and thus represent potential parthanatic downstream mediators of HtrA2/Omi. Moreover, mass-spectrometric screening for novel parthanatic substrates of HtrA2/Omi revealed that the induction of parthanatos does not cause a substantial proteolytic cleavage or major alterations in the abundance of mitochondrial proteins. Resolving these findings, reconstitution of HtrA2/Omi-deficient cells with a catalytically inactive HtrA2/Omi mutant restored their sensitivity against parthanatos to the same level as the protease-active HtrA2/Omi protein. Additionally, an inhibitor of HtrA2/Omi's protease activity did not confer protection against parthanatic cell death. Our results demonstrate that HtrA2/Omi controls parthanatos in a protease-independent manner, likely via novel, unanticipated functions as a scaffolding protein and an interaction with so far unknown mitochondrial proteins. - Source: PubMed
Publication date: 2023/08/18
Weiß JonasHeib MichelleKorn ThiemoHoyer JustusFuchslocher Chico JohaiberVoigt SusannKoudelka TomasTholey AndreasAdam Dieter - - Source: PubMed
Publication date: 2023/04/27
De Santis TizianaSerpieri ValentinaBiagini TommasoLanotte MicheleCriffò CarlottaMazza TommasoValente Enza MariaAlbanese Alberto