StressMarq蚂蚁淘在线

StorageBuffer	Na-Phosphate,pH7.5(20mM),150mMNaCl,10%glycerol,200mMImidazole
StorageTemperature	-20ºC
ShippingTemperature	BlueIceor4ºC
Purification	AffinityPurified
Specificity	~70kDa
CiteThisProduct	HumanRecombinantHSP70Protein(StressMarqBiosciencesInc.,VictoriaBCCANADA,Catalog#SPR-103)
CertificateofAnalysis	Thisproducthasbeencertified>90%pureusingSDS-PAGEanalysis.TheproteinhasATPaseactivityatthetimeofmanufactureof3.3µMphosphateliberated/hr/µgproteinina200µlreactionat37°C(pH7.5)inthepresenceof20ulof1mMATPusingaMalachiteGreenassay.

BIOLOGicalDescription

AlternativeNames	HSP701Protein,HSP702Protein,HSP70.1Protein,HSP72Protein,HSP73Protein,HSPA1Protein,HSPA1AProtein,HSPA1BProtein
ResearchAreas	Cancer,HeatShock
CellularLocalization	Cytoplasm
AccessionNumber	NM_005345
GeneID	3303
SwissProt	P08107
ScientificBackground	HSP70genesencodeabundantheat-inducIBLe70-kDaHSPs(HSP70s).InmosteukaryotesHSP70genesexistaspartofamultigenefamily.Theyarefoundinmostcellularcompartmentsofeukaryotesincludingnuclei,mitochondria,chloroplasts,theendoplasmicreticulumandthecytosol,aswellasinbacteria.Thegenesshowahighdegreeofconservation,havingatleast50%identity(2).TheN-terminaltwothirdsofHSP70saremoreconservedthantheC-terminalthird.HSP70bindsATPwithhighaffinityandpossessesaweakATPaseactivitywhichcanbestimulatedbybindingtounfoldedproteinsandsyntheticpeptides(3).WhenHSC70(constitutivelyexpressed)presentinmammaliancellswastruncated,ATPbindingactivitywasfoundtoresideinanN-terminalfragmentof44kDawhichlackedpeptidebindingcapacity.PolypeptidebindingABIlitythereforeresidedwithintheC-terminalhalf(4).ThestructureofthisATPbindingdomaindisplaysmultiplefeaturesofnucleotidebindingproteins(5).AllHSP70s,regardlessoflocation,bindproteins,particularlyunfoldedones.ThemolecularchaperonesoftheHSP70familyrecognizeandbindtonascentpolypeptidechainsaswellaspartiallyfoldedintermediatesofproteinspreventingtheiraggregationandmisfolding.ThebindingofATPtriggersacriticalconformationalchangeleADIngtothereleaseoftheboundsubstrateprotein(6).TheuniversalabilityofHSP70stoundergocyclesofbindingtoandreleasefromhydrophobicstretchesofpartiallyunfoldedproteinsdeterminestheirroleinagreatvarietyofvitalintracellularfunctionssuchasproteinsynthesis,proteinfoldingandoligomerizationandproteintransport.LookingformoreinformationonHSP70?VisitournewHSP70ScientificResourceGuideathttp://www.HSP70.com.
References	1.ZhoJ.(1998)Cell.94:471-480. 2.Boorstein,W.R.,Ziegelhoffer,T.&Craig,E.A.(1993)J.Mol.Evol.38(1):1-17. 3.RothmanJ.(1989)Cell.59:591-601. 4.DeLuca-Flahertyetal.(1990)Cell.62:875-887. 5.BorkP.,SanderC.&ValenciaA.(1992)Proc.NatlAcad.Sci.USA.89:7290-7294. 6.FinkA.L.(1999)Physiol.Rev.79:425-449. 7.SmithD.F.,etal.,(1993)Mol.Cell.Biol.13(2):869-876. 8.PrapapanichV.,etal.,(1996)Mol.Cell.Biol.16(11):6200-6207. 9.Fernandez-Funezetal.,(2000)Nature.408(6808):101-106.

ProductImages

SDS-PAGEof70kDaHsp70protein(SPR-103).

ProductCitations(7)

ELISA

MeasuringHsp72(HSPA1A)byIndirectSandwichELISA.

Ireland,H.E.andWilliams,J.H.H.(2011)MethodsMolBiol.787,145-153.

PubMedID:21898234Applications:ELISA

TheDangerSignalS100BIntegratesPathogen–andDanger–SensingPathwaystoRestrainInflammation.

Sorci,G.etal.(2011)PLoSPathog.7(3):e1001315.

PubMedID:21423669Applications:ELISA

OtherCitations

Re-examiningHSPC1inhibitors.

Lee,S.L.etal.(2017)CellStressChaperones.22(2):293-306.

PubMedID:28255900Applications:WesternBlotControl

Hsp70PromotesEpithelialSodiumChannelFunctionalExpressionbyIncreasingItsAssociationwithCoatComplexIIandItsExitfromEndoplasmicReticulum.

Chanoux,R.A.etal.(2012)JBiolChem.287.19255-19265.

PubMedID:22496374Applications:WesternBlotControl

IdentificationofthemajorallergenofMalasseziaglobosarelevantforatopicdermatitis.

Ishibashi,Y.,Kato,H.,Asahi,Y.,Suqita,T.andNishikawa,A.(2009)JDermatolSci.55(3):185-192.

PubMedID:19540092Applications:WesternBlotInhibitor

InVivoGenerationofNeurotoxicPrionProtein:RoleforHsp70inAccumulationofMisfoldedIsoforms.

Fernandez-Funez,P.etal.(2009)PLoSGenet.5(6):e1000507.

PubMedID:19503596Applications:Immunoprecipitation

IdentificationofPhosphorylation-DependentBindingPartnersofAquaporin-2UsingProteinMassSpectrometry.

Zwang,N.A.etal.(2009)JProteomeRes.8(3):1540-1554.

PubMedID:19209902Applications:WesternBlotControl

StressMarq细胞信号生物体中的每个细胞都暴露于来自其环境的数百种不同信号。单元可以以多种方式响应这些信号，并且独立地响应。但是，所有这些独立的动作在控制基本细胞活动的非常复杂且相互联系的通信路径中融合在一起。细胞外信号通过各种信号网络传输信息，最终在细胞核水平发挥作用。小区信令或蜂窝通信的三个阶段包括：接收信号信号转导单元内的响应倾向于起源于质膜水平的信号传导途径或网络包括G蛋白偶联受体，（非受体）酪氨酸激酶和离子调节通道等。尽管这些过程中涉及的关键调节分子有所不同，但信号的传输通常涉及一个共同的过程。靶蛋白的可逆磷酸化。两种不同的酶介导了这一点：蛋白激酶–磷酸化蛋白质（添加磷酸基团）蛋白质磷酸酶–使蛋白质脱磷酸（去除磷酸基团）细胞感知并正确响应其微环境的能力是发育，组织修复，免疫以及正常组织动态平衡的基础。细胞内信号传导事件实际上调节了所有细胞活动。细胞信息处理中的错误可能导致癌症，自身免疫性疾病和糖尿病等疾病。通过了解细胞信号传导的基本原理，研究人员希望能够开发出新药并对其进行选择性和有效治疗。细胞信号研究需要大量的生命科学产品。我们致力于开发最先进的研究产品，以协助研究细胞信号传导，包括单克隆抗体，多克隆抗体，抗体结合物，蛋白质，免疫测定法和小分子抑制剂。

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