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HSPA8/HSC70  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: E. coli  
50 µg 
100 µg 
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HSPA8/HSC70 Related Area

HSPA8/HSC70 Related Pathways

    HSPA8/HSC70 Summary & Protein Information

    HSPA8/HSC70 Background

    Gene Summary: HSPA8 gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This HSC70 protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. HSC70 protein functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
    General information above from NCBI
    Subunit structure: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7 and DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with SV40 VP1. Interacts with TRIM5. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PARK2. Interacts with FOXP3. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11147964, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:16815975, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:20053985, ECO:0000269|PubMed:23865999, ECO:0000269|PubMed:23921388, ECO:0000269|PubMed:23973223, ECO:0000269|PubMed:23990462, ECO:0000269|PubMed:24270810, ECO:0000269|PubMed:9305631, ECO:0000269|PubMed:9679980}.
    Domain: The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain. {ECO:0000269|PubMed:9305631}.
    Subcellular location: Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
    Tissue specificity: Ubiquitous. {ECO:0000269|PubMed:11276205}.
    Induction: Constitutively synthesized.
    Post-translational: Acetylated. {ECO:0000269|Ref.5, ECO:0000269|Ref.6}.; ISGylated. {ECO:0000269|PubMed:16139798, ECO:0000269|PubMed:16815975}.; Trimethylation at Lys-561 reduces fibrillar SNCA binding.
    Sequence similarity: Belongs to the heat shock protein 70 family. {ECO:0000305}.
    General information above from UniProt

    HSPA8, also known as HSC70, is a member of the heat shock protein family due to homology with other heat shock proteins. The heat shock protein 70 family is comprised by both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. HSPA8 belongs to the heat-shock cognate subgroup. Members of the human heat-shock protein multigene family have several highly conserved proteins with structural and functional properties in common, but vary in the extent of their inducibility in response to metabolic stress. HSPA8 is constitutively expressed and performs functions related to normal cellular processes. This protein binds to nascent polypeptides to facilitate correct protein folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Two alternatively spliced variants have been characterized to date. HSPA8 acts as a repressor of transcriptional activation. It inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones. It also is a ATPase that works with auxilin to remove clathrin coated vesicles. In neurons, synaptojanin is also an important protein involved in vesicle uncoating.

    HSPA8/HSC70 Alternative Name

    LAP1,HSC54,HSC70,HSC71,HSP71,HSP73,LAP-1,NIP71,HEL-33,HSPA10,HEL-S-72p, [homo-sapiens]
    HSC54,HSC70,HSP71,HSP73,HSPA10,HSPA8,LAP1,MGC131511,MGC29929,HSC71,NIP71, [human]
    Hsc70,Hspa8,MGC114311, [mouse]
    Hsc70,Hsc71,Hsc73,Hsp73,Hspa10,2410008N15Rik, [mus-musculus]

    HSPA8/HSC70 Related Studies

  • Santacruz H, et al. (1997) Molecular characterization of a heat shock cognate cDNA of zebrafish, hsc70, and developmental expression of the corresponding transcripts. Dev Genet. 21:223-33.
  • Harhay G P, et al. (2005) Characterization of 954 bovine full-CDS cDNA sequences. BMC Genomics. 6: 166.
  • Goldfarb S, et al. (2006) Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels. Proc Natl Acad Sci. 103(15):5817-22.