HSC70 Antibody (YA6426)

Cat. No.: HY-P86734: Ficha de datos COA
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HSC70 Antibody (YA6426) is a Mouse-derived and non-conjugated IgG monoclonal antibody, targeting to HSC70.

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Tamaño	Stock	Cantidad
10 μL	En stock	Estimated Time of Arrival: December 31
50 μL	En stock	Estimated Time of Arrival: December 31
100 μL	En stock	Estimated Time of Arrival: December 31
250 μL	Obtener un presupuesto

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Verification Image
Background
Descripciòn

Descripciòn

HSC70 Antibody (YA6426) is a Mouse-derived and non-conjugated IgG monoclonal antibody, targeting to HSC70.

Host

Mouse

Clonality

Monoclonal

Peso molecular

Predicted band size: 71 kDa

Species Reactivity

Human, Mouse, Rat

SwissProt ID

P11142

Gene ID

3312 [NCBI]

Immunogen

Recombinant human HSC70 Protein

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:500-1000
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:100-500
IHC-F IHC-F: Immunohistochemistry-Frozen	1:100-500
ICC/IF ICC/IF: Immunocytochemistry/Immunofluorescence	1:100-500

Pureza	affinity purified.	Conjugation	Non-conjugated
Modification	Unmodified	Isotype	IgG

Appearance

Liquid

Formulation

Supplied in 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Storage & Stability

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

Envío

Shipping with blue ice.

Verification Image

Western blot analysis was performed on protein extracts (25 μg) from HeLa (lane 2), 293T (lane 3), HT-1080 (lane 4), Caco-2 (lane 5), A549 (lane 6) and THP-1 (lane 7) using HSC70 antibody. Proteins were transferred onto a 0.45 μm PVDF membrane using the Trans-Blot^® Turbo^™ system for 13 min. The membrane was then blocked with 5% nonfat milk in TBST (HY-K1025) for 1 h at room temperature. Thhe primary antibody (1:1000) and loading control antibody GAPDH Antibody (HRP) (HY-P80954A) (1:2500) were diluted in 5% nonfat milk in TBST and incubated with the membrane overnight at 4°C. After washing, the membrane of primary antibody was incubated with HRP-conjugated goat anti-rabbit/mouse IgG secondary antibody (HY-P8001/HY-P8004) (1:5000) diluted in 5% nonfat milk in TBST for 1 h at room temperature. Protein bands were visualized using an Ultra High Sensitivity ECL detection kit (HY-K1005).

Background

Function：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 (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). 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 (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). 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 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). 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 (PubMed:10722728, PubMed:11276205). 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 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). 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 (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). 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 (By similarity)

Subcellular Localization：Cytoplasm,Melanosome,Nucleus, nucleolus,Cell membrane,Lysosome membrane

Expression：
Tissue_Specificity: Ubiquitous
Induction: Constitutively synthesized

Isoforms & Post-Translational Modification：P11142 has two isomers: P11142-1: 70898 Da (predicted); P11142-2: 53518 Da (predicted).
Acetylated丨ISGylated丨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)

Synonyms

2410008N15Rik; Constitutive heat shock protein 70; Heat shock 70 kDa protein 8; Heat shock 70kD protein 10; Heat shock 70kD protein 8; Heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; Heat shock cognate protein 54; Heat shock cognate protein 71 kDa; Heat shock protein 8; Heat shock protein A8; Heat-shock70-KD protein 10, formerly; HSC54; HSC71; Hsc73; HSP71; HSP73; HSP7C_HUMAN; HSPA10; HSPA8; LAP1; Lipopolysaccharide associated protein 1; LPS associated protein 1; LPS associated protein; MGC102007; MGC106514; MGC114311; MGC118485; MGC131511; MGC29929; N-myristoyltransferase inhibitor protein 71; NIP71; HSC 70; HSC-70.

Documentación

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