Anti-Hsp70 Antibody |产品详情|进口试剂采购网

您好，欢迎来到拜力生物网站！请登录注册

我的订单 | 联系我们 | 在线客服QQ：3012681483 | 客服电话：400-968-7988 | 工作时间：08:30-17:30

主营产品： ELISA试剂盒、抗体、补体血清、兔补体、干扰素、小鼠测温仪、进口试剂、Quidel代理、Swant代理、PBL Assay Science代理

网站首页产品中心代理品牌新闻资讯资源中心关于我们

所在位置：首页 > 产品中心 > Antibodies > Antibodies产品

订购信息

上海拜力生物科技公司

Tel:400-968-7988 021-33779008

Anti-Hsp70 Antibody

品牌：Antibodies

货号：

规格：50µl

货期：

应用：

咨询客服

立即购买加入购物车

Anti-Hsp70 Antibody

商品详情参考文献相关资料

Overview

Name:	Anti-Hsp70 Antibody See all Hsp70 primary antibodies
Description:	Rabbit monoclonal antibody to Hsp70
Specificity:	This antibody detects endogenous levels of Hsp70 and does not cross-react with related proteins.
Applications:	WB, ICC/IF, IHC, FC
Reactivity:	Human, Mouse, Rat
Immunogen:	Recombinant antibody.
Host:	Rabbit
Clonality:	Monoclonal
Conjugate:	Unconjugated
Molecular Weight:	~ 70 kDa
Purity:	Protein A affinity purified
Product Form:	Recombinant Rabbit Monoclonal Antibody. 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.

Target

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, 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:26865365, PubMed:24318877). 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).
Tissue Specificity:	HSPA1B is testis-specific.
Sequence Similarities:	Belongs to the heat shock protein 70 family.
Post-Translational Modification:	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.
Cellular Location:	Cytoplasm. Cytoplasm > Cytoskeleton > Microtubule organizing center > Centrosome. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Database Links:	Entrez Gene: 3303?Human Entrez Gene: 3304?Human Entrez Gene: 15511?Mouse Entrez Gene: 193740?Mouse Entrez Gene: 24472?Rat Entrez Gene: 294254?Rat Omim: 140550?Human Omim: 603012?Human SwissProt: P08107?Human SwissProt: P0DMV8?Human SwissProt: P0DMV9?Human SwissProt: P17879?Mouse SwissProt: Q61696?Mouse SwissProt: Q07439?Rat Unigene: 274402?Human Unigene: 719966?Human Unigene: 728810?Human Unigene: 1950?Rat Unigene: 228225?Rat
Synonyms:	DnaK type molecular chaperone HSP70 1 Antibody Epididymis secretory protein Li 103 Antibody FLJ54303 Antibody FLJ54370 Antibody FLJ54392 Antibody FLJ54408 Antibody FLJ75127 Antibody Heat shock 70 kDa protein 1 Antibody Heat shock 70 kDa protein 1/2 Antibody Heat shock 70 kDa protein 1A/1B Antibody Heat shock 70kDa protein 1A Antibody Heat shock 70kDa protein 1B Antibody Heat shock induced protein Antibody HEL S 103 Antibody Hsp70 Antibody HSP70 1 Antibody HSP70 1/HSP70 2 Antibody HSP70 1B Antibody HSP70 2 Antibody HSP70 iA Antibody HSP70-1/HSP70-2 Antibody HSP70-1A Antibody HSP70.1 Antibody HSP70.1/HSP70.2 Antibody HSP70I Antibody HSP71_HUMAN Antibody HSP72 Antibody HSPA1 Antibody HSPA1A Antibody HSPA1B Antibody
Information:	Target information shown above is from the UniProt Consortium.