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- 2025年10月15日
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50T
| 产品编号 | IHC0453 |
| 英文名称 | HSP70 Ready-To-Use IHC Kit |
| 中文名称 | 热休克蛋白-70即用型免疫组化试剂盒 |
| 英文别名 | 70kDa; 87A; AI317151; APG-2; APG2; Bb; CG18743; CG31359; CG31366; CG31449; CG6489; dHSP70; dhsp70Aa; Dm-hsp70; Dmel\CG31359; Dmel\CG31366; Dmel_CG31359; Dmel_CG31366; DmHSP70AA; DMHSP7D1; Hcp70.1; Hcp70.2; HEL-S-103; HEL-S-5a; HS24/P52; hs70; Hsc70t; HSP 70; Hsp-70; Hsp-70Aa; Hsp110; hsp68; HSP70; hsp70 87A; hsp70 87C; hsp70 Aa; hsp70(87A); Hsp70(87C); HSP70-1; HSP70-1A; HSP70-1B; HSP70-1L; HSP70-2; HSP70-3; HSP70-HOM; HSP70.1; HSP70.2; Hsp70.3; Hsp70A; Hsp70A1; HSP70A2; Hsp70A7d; Hsp70Aa; Hsp70Ab; Hsp70B; Hsp70Ba; Hsp70Bb; Hsp70Bbc; Hsp70Bc; HSP70I; Hsp70RY; HSP70T; HSP72; HSPA1; HSPA1A; HSPA1B; HSPA1L; HSPA2; HSPA4; HSPH2; Hspt70; Hst70; HSX70; hum70t; Irp94; mKIAA4025; Msh5; RY |
| 产品应用 | IHC-P Not yet tested in other applications. |
| 交叉反应 | Human, Mouse, Rat |
| 亚基 | May be an auxiliary component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (PubMed:12853476, PubMed:15383005, PubMed:15963462, PubMed:17233114, PubMed:18620420, PubMed:21081504). Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain) (PubMed:20053985). Interacts with METTL21A (PubMed:23921388). Interacts with PRKN (PubMed:24270810). Interacts with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J domain) (PubMed:17182002, PubMed:33857403). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes (PubMed:22528486). Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively (PubMed:27708256). Interacts with NEDD1 (PubMed:27137183). Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105 (PubMed:24318877). Interacts with SMAD3 (PubMed:24613385). Interacts with DNAJC8 (PubMed:27133716). |
| 亚细胞定位 | #Cytoplasm #Cytoskeleton |
| 组织特异性 | HSPA1B is testis-specific. |
| 翻译后修饰 | In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress. |
| 相似性 | Belongs to the heat shock protein 70 family. |
| 功能 | Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. 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, 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 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as 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:24012426, PubMed:24318877, PubMed:26865365). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cel |
| 保存条件 | Please store components at the temperatures indicated on the individual tube labels. The kit is stable for 6 months from the date of receipt. |
| 背景资料 | HSP70 is a Heat shock protein (HSP) which are expressed in response to various biological stresses, including high temperatures. There are several major families of HSPs that include HSP70, there are HSP90 and HSP100. The HSP70 family is a set of highly conserved proteins that are induced by a variety of biological stresses, including heat stress, in every organism in which the proteins have been examined. The human HSP70 family members include: HSP70, a protein which is strongly inducible in all organisms but which is also constitutively expressed in primate cells; HSP72, a 72 kDa protein that is induced exclusively under stress conditions; HSC70, or cognate protein, is a 72 kDa, constitutively expressed, protein which is involved in the uncoating of clathrin coated vesicles; GRP78, or BiP, is a glucose regulated 78 kDa protein localized in the endoplasmic reticulum; and p75, or HSP75, a 75 kDa protein that is found within the mitochondria. Further, HSP70 is encoded by an intronless gene and, in conjunction with other heat shock proteins, HSP70 stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and organelles. HSP70 is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The HSP70 gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. |
| 应用 | 推荐稀释比例 |
Immunohistochemical analysis of paraffin embedded rat testis tissue slide using IHC0453 (HSP70 IHC Kit).
Immunohistochemical analysis of paraffin embedded human testis tissue slide using IHC0453 (HSP70 IHC Kit).
Immunohistochemical analysis of paraffin embedded mouse testis tissue slide using IHC0453 (HSP70 IHC Kit).
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HSP70 Ready-To-Use IHC Kit(IHC0453)-50T
￥3200
