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HSC70 Antibody (YA360)

(Synonyms: Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8))
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Based on 1 publication(s) in Google Scholar

HSC70 Antibody (YA360) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to HSC70.

For research use only. We do not sell to patients.
  • Host:

    Rabbit

  • Isotype:

    IgG

  • Application:

    WB, IHC-P, IP

  • Reactivity :

    Human, Mouse, Rat, Hamster

  • Formulation:

    Supplied in 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol and 0.05% BSA. Preservative: 0.01% Sodium azide

  • Conjugation:
    Non-conjugated
  • Experimental Validation Results for HSC70 Antibody (YA360)
  • Experimental Validation Results for HSC70 Antibody (YA360)
  • HSC70 Antibody (YA360) Product Image
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Applications

Application
WB Info
WB: Western Blot
IHC-P Info
IHC-P: Immunohistochemistry-Paraffin
IP Info
IP: Immunoprecipitation
Dilution Ratio 1:500-1:1000 1:50-1:100 1:20

Product Details

제품 설명

HSC70 Antibody (YA360) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to HSC70.

  • Host Rabbit
  • Clonality Recombinant,Monoclonal
  • Species Reactivity
    Human, Mouse, Rat, Hamster
  • Observed Molecular Weight
    Observed band size: 71 kDa Info
    Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
  • Calculated Molecular Weight Predicted band size: 71 kDa
Species Reactivity Database
Immunogen

Synthetic peptide corresponding to Human Hsc70 aa622-636.

Sensitivity

Endogenous

Purification

affinity purified

Conjugation

Non-conjugated

Modification

Unmodified

Isotype

IgG

RRID

AB_3102164

Product Properties

  • Appearance

    Solution

  • Formulation

    Supplied in 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol and 0.05% BSA. Preservative: 0.01% Sodium azide

  • Concentration

    Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration

  • Storage & Stability

    Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

  • 선적

    Shipping with blue ice.

Verification Images

  • Experimental Validation Results for HSC70 Antibody (YA360)
    Western blot analysis of extracts from NIH/3T3(lane 2(20ug) ,Hela(lane 3(20ug) and A431(lane 4(20ug) using Hsc70 Antibody (HY-P80708) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P83730, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
  • Experimental Validation Results for HSC70 Antibody (YA360)
    Western blot analysis was performed on extracts from Hela (lane 1, 15 μg), 293 (lane 2, 15 μg), NCI-H1299 (lane 3, 15 μg), 3T3 (lane 4, 15 μg), C6 (lane 5, 15 μg), and PC-12 (lane 6, 15 μg) using Hsc70 Rabbit mAb.Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST at 4°C overnight.The primary antibody (1:1000 dilution) and the loading control antibody (GAPDH, HY-P80137, 1:20000 dilution) were incubated in 5% non-fat milk in TBST for 1 hour at 37°C.Goat Anti-Rabbit IgG-HRP Secondary Antibody (1:20000 dilution) was then applied for 40 minutes at 37°C.

Background

  • Function

    HSC70 is a Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17].

  • Subcellular Localization

    Cytoplasm; Melanosome; Nucleus, nucleolus; Cell membrane; Lysosome membrane; Peripheral membrane protein; Cytoplasmic side

  • Expression


    Tissue_specificity:general expression

    Induction:Constitutively synthesized

  • Isoforms & Post-Translational Modification

    P11142 has 2 isomers: P11142-1: 70898 Da (predicted); P11142-2: 53518 Da (predicted).
    Acetylated;ISGylated;Trimethylation at Lys-561 reduces fibrillar SNCA binding

  • Subunit

    Component of the chaperone-assisted selective autophagy (CASA) complex consisting of BAG3, HSPA8/HSC70, HSPB8 and STUB1/CHIP (PubMed:20060297). 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. Interacts with DNAJB12 (via J domain) (PubMed:21148293, PubMed:21150129, PubMed:24732912, PubMed:27916661). Interacts with DNAJB14 (via J domain) (PubMed:23018488, PubMed:24732912, PubMed:27916661). 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 TRIM5. Part of a complex composed at least of ASH2L, 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 PRKN. Interacts with FOXP3. Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with MLLT11 (PubMed:24880125). Interacts with RNF207 (PubMed:25281747). Interacts with DNAJC21 (PubMed:27346687). Interacts with DNAJB2 (PubMed:15936278). Interacts with TTC1 (via TPR repeats) (PubMed:15708368). Interacts with SGTA (via TPR repeats) (By similarity). Interacts with HSF1 (via transactivation domain) (PubMed:9499401). Interacts with HOPX, HSP40 and HSP90 (PubMed:27708256). Component of the chaperone-assisted selective autophagy (CASA) complex consisting of BAG3, HSPA8/HSC70, HSPB8 and STUB1/CHIP (PubMed:20060297). Interacts with STUB1 (PubMed:27708256). Interacts with BAG2 (PubMed:24318877). Interacts with BAG3 (PubMed:24318877, PubMed:27474739). Interacts with DNAJC12 (PubMed:24122553). Interacts with ZMYND10 (PubMed:29601588). Interacts with HSPC138 (PubMed:25760597). Interacts with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is impaired in the absence of GIMAP5 (By similarity). Interacts with NLPR12 (PubMed:17947705). Interacts with TTC4 (PubMed:18320024). Interacts with TOMM70; the interaction is required for preprotein mitochondrial import (PubMed:12526792). May interact with DNJC9; the interaction seems to be histone-dependent (PubMed:33857403). Interacts with BAG5 and JPH2; the interaction with JPH2 is increased in the presence of BAG5 (PubMed:35044787). Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328). Interacts with molecular chaperone MIPEP155 (via N-terminal ATP-binding region); the interaction results in reduced ATPase activity of HSPA8, impaired interaction of HSPA8 with HSP90 and reduced lysosomal antigen trafficking (PubMed:32671205). Interacts with CDKN1B; the interaction may be associated with susceptibility to ubiquitination (PubMed:26775844). Interacts with HTN3 peptide Hst3; the interaction enhances HSPA8-CDKN1B complex formation (PubMed:26775844). Interacts with DNAJC6 (via J domain) in an ATP-dependent manner; this interaction stimulates the HSPA8's ATPase activity. Forms a complex composed of HSPA8, CLTC and DNAJC6 (By similarity). Interacts with HSPA8; this interaction modulates migratory and antigen-presenting capacities of dendritic cells (PubMed:17785435, PubMed:20060297)

  • SwissProt ID

    P11142

  • Gene ID
    3312 [NCBI]
  • Synonyms

    Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)

  • Research Field

    Signal Transduction

[1]. Grove DE, et al. The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508. Mol Biol Cell. 2011 Feb 1;22(3):301-14. [Content Brief]

[2]. Yamamoto YH, et al. A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR. Cell Struct Funct. 2010;35(2):107-16. [Content Brief]

[3]. Sopha P, et al. A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins. Cell Struct Funct. 2012;37(2):177-87. [Content Brief]

[4]. Goodwin EC, et al. Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure. PLoS One. 2014;9(4):e94322. [Content Brief]

[5]. Li K, et al. Tetrameric Assembly of K(+) Channels Requires ER-Located Chaperone Proteins. Mol Cell. 2017 Jan 5;65(1):52-65. [Content Brief]

[6]. Chiang HL, et al. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science. 1989 Oct 20;246(4928):382-5. [Content Brief]

[7]. Wang L, et al. Palmitoylation prevents sustained inflammation by limiting NLRP3 inflammasome activation through chaperone-mediated autophagy. Mol Cell. 2023 Jan 19;83(2):281-297.e10. [Content Brief]

[8]. Young JC, et al. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell. 2003 Jan 10;112(1):41-50. [Content Brief]

[9]. Stricher F, et al. HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting. Autophagy. 2013 Dec;9(12):1937-54. [Content Brief]

[10]. Rauch JN, et al. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J Biol Chem. 2014 Jan 17;289(3):1402-14. [Content Brief]

[11]. Radons J, et al. The human HSP70 family of chaperones: where do we stand?. Cell Stress Chaperones. 2016 May;21(3):379-404. [Content Brief]

[12]. Rauch JN, et al. Non-canonical Interactions between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release. J Biol Chem. 2016 Sep 16;291(38):19848-57. [Content Brief]

[13]. Yahata T, et al. The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors. J Biol Chem. 2000 Mar 24;275(12):8825-34. [Content Brief]

[14]. Triantafilou K, et al. A CD14-independent LPS receptor cluster. Nat Immunol. 2001 Apr;2(4):338-45. [Content Brief]

[15]. Agarraberes FA, et al. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci. 2001 Jul;114(Pt 13):2491-9. [Content Brief]

[16]. Zhou D, et al. Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity. 2005 May;22(5):571-81. [Content Brief]

[17]. Matsumura Y, et al. Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase. J Biol Chem. 2013 Oct 25;288(43):31069-79. [Content Brief]

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HSC70 Antibody (YA360) Related Classifications

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100 mg

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Measured by its ability to inhibit anti-CD3-induced proliferation of stimulated CTLL-2 mouse cytotoxic T cells. The ED50 this effect is 0.8023 μg/ml, corresponding to a specific activity is 1246.42 units/mg.

Assay Types
  • 1/16

    MedchemExpress Validation
     Western blot analysis of extracts from NIH/3T3(lane 2(20ug) ,Hela(lane 3(20ug) and A431(lane 4(20ug) using Hsc70 Antibody (HY-P80708) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P83730, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.

  • 1/16

    MedchemExpress Validation
     Western blot analysis was performed on extracts from Hela (lane 1, 15 μg), 293 (lane 2, 15 μg), NCI-H1299 (lane 3, 15 μg), 3T3 (lane 4, 15 μg), C6 (lane 5, 15 μg), and PC-12 (lane 6, 15 μg) using Hsc70 Rabbit mAb.Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST at 4°C overnight.The primary antibody (1:1000 dilution) and the loading control antibody (GAPDH, HY-P80137, 1:20000 dilution) were incubated in 5% non-fat milk in TBST for 1 hour at 37°C.Goat Anti-Rabbit IgG-HRP Secondary Antibody (1:20000 dilution) was then applied for 40 minutes at 37°C.

  • HSC70 Antibody (YA360) Product Image
    1/16
  • Experimental Validation Results for HSC70 Antibody (YA360)
  • Experimental Validation Results for HSC70 Antibody (YA360)
  • HSC70 Antibody (YA360) Product Image
  • Experimental Validation Results for HSC70 Antibody (YA360)
    1/1
    MedchemExpress Validation
     Western blot analysis of extracts from NIH/3T3(lane 2(20ug) ,Hela(lane 3(20ug) and A431(lane 4(20ug) using Hsc70 Antibody (HY-P80708) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P83730, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
  • Experimental Validation Results for HSC70 Antibody (YA360)
    1/1
    MedchemExpress Validation
     Western blot analysis was performed on extracts from Hela (lane 1, 15 μg), 293 (lane 2, 15 μg), NCI-H1299 (lane 3, 15 μg), 3T3 (lane 4, 15 μg), C6 (lane 5, 15 μg), and PC-12 (lane 6, 15 μg) using Hsc70 Rabbit mAb.Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST at 4°C overnight.The primary antibody (1:1000 dilution) and the loading control antibody (GAPDH, HY-P80137, 1:20000 dilution) were incubated in 5% non-fat milk in TBST for 1 hour at 37°C.Goat Anti-Rabbit IgG-HRP Secondary Antibody (1:20000 dilution) was then applied for 40 minutes at 37°C.
  • Experimental Validation Results for HSC70 Antibody (YA360)
  • Experimental Validation Results for HSC70 Antibody (YA360)
  • HSC70 Antibody (YA360) Product Image
    MedchemExpress Validation

    Western blot analysis of extracts from NIH/3T3(lane 2(20ug) ,Hela(lane 3(20ug) and A431(lane 4(20ug) using Hsc70 Antibody (HY-P80708) Rabbit mAb. Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P83730, 1/10000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.

  • HSC70 Antibody (YA360) Product Image
    MedchemExpress Validation

    Western blot analysis was performed on extracts from Hela (lane 1, 15 μg), 293 (lane 2, 15 μg), NCI-H1299 (lane 3, 15 μg), 3T3 (lane 4, 15 μg), C6 (lane 5, 15 μg), and PC-12 (lane 6, 15 μg) using Hsc70 Rabbit mAb.Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST at 4°C overnight.The primary antibody (1:1000 dilution) and the loading control antibody (GAPDH, HY-P80137, 1:20000 dilution) were incubated in 5% non-fat milk in TBST for 1 hour at 37°C.Goat Anti-Rabbit IgG-HRP Secondary Antibody (1:20000 dilution) was then applied for 40 minutes at 37°C.

  • HSC70 Antibody (YA360) Product Image WB
  • HSC70 Antibody (YA360) Product Image WB