Recombinant Human HSPC142 protein is a Human Full Length protein, in the 1 to 329 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S M E V A E P S S P T E E E E E E E E H S A E P R P R T R S N P E G A E D R A V G A Q A S V G S R S E G E G E A A S A D D G S L N T S G A G P K S W Q V P P P A P E V Q I R T P R V N C P E K V I I C L D L S E E M S L P K L E S F N G S K T N A L N V S Q K M I E M F V R T K H K I D K S H E F A L V V V N D D T A W L S G L T S D P R E L C S C L Y D L E T A S C S T F N L E G L F S L I Q Q K T E L P V T E N V Q T I P P P Y V V R T I L V Y S R P P C Q P Q F S L T E P M K K M F Q C P Y F F F D V V Y I H N G T E E K E E E M S W K D M F A F M G S L D T K G T S Y K Y E V A L A G P A L E L H N C M A K L L A H P L Q R P C Q S H A S Y S L L E E E D E A I E V E A T V
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985).
C19orf62, MERIT40, NBA1, HSPC142, BABAM1, BRISC and BRCA1-A complex member 1, Mediator of RAP80 interactions and targeting subunit of 40 kDa, New component of the BRCA1-A complex
Recombinant Human HSPC142 protein is a Human Full Length protein, in the 1 to 329 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl
ab183249 is purified by using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.
Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985).
Belongs to the BABAM1 family.
HSPC142 also called CCDC53 is a protein involved mechanically in several cellular processes. It weighs approximately 38 kDa and is expressed broadly in many tissues. HSPC142 plays a significant role in the regulation of cytoskeletal dynamics suggesting it is important in maintaining cellular integrity. Researchers often study HSPC142 to understand its localization and interactions within different cellular compartments.
HSPC142 contributes to the organization and function of the actin cytoskeleton. It forms part of the WASH (Wiskott-Aldrich syndrome protein and SCAR homolog) complex which is important for actin nucleation. This complex works with other proteins to facilitate processes like endosomal sorting and membrane trafficking. It aids in maintaining proper cellular function by influencing actin filament assembly and disassembly.
Researchers recognize HSPC142’s role in the regulation of the Arp2/3 complex pathway and the WASH pathway. Here HSPC142 interacts with proteins such as WASH1 and F-actin driving changes in the cytoskeleton necessary for cellular transport activities. These interactions ensure that cells can move materials efficiently indicating a broader impact on cellular homeostasis and signaling processes.
Studies link HSPC142 to neurodegenerative conditions and cancers. Disruptions in its function can lead to abnormal cell migration and changes in the brain's cellular architecture. In Alzheimer's disease models alterations in cytoskeletal dynamics due to faulty HSPC142 pathways show significant connections with tau proteins. In cancer unregulated HSPC142 activity associates with increased cell invasion and metastasis implicating other proteins like WAVE2 in these transformative processes.
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15% SDS PAGE analysis of ab183249 (3μg).
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