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Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)

 HS71A_RAT               Reviewed;         641 AA.
P0DMW0; P42853; Q07439; Q63256;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
27-MAY-2015, sequence version 1.
02-JUN-2021, entry version 49.
RecName: Full=Heat shock 70 kDa protein 1A;
AltName: Full=Heat shock 70 kDa protein 2;
Short=HSP70-2;
Short=HSP70.2;
Name=Hspa1a; Synonyms=Hsp70-1, Hspa1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LEW.1W/GUN;
PubMed=7927536; DOI=10.1007/bf01246673;
Walter L., Rauh F., Guenther E.;
"Comparative analysis of the three major histocompatibility complex-linked
heat shock protein 70 (Hsp70) genes of the rat.";
Immunogenetics 40:325-330(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15060004; DOI=10.1101/gr.1987704;
Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
"The genomic sequence and comparative analysis of the rat major
histocompatibility complex.";
Genome Res. 14:631-639(2004).
-!- 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.
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. 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. Enhances STUB1-
mediated SMAD3 ubiquitination and degradation and facilitates STUB1-
mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated
ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg)
during inflammation. Negatively regulates heat shock-induced HSF1
transcriptional activity during the attenuation and recovery phase
period of the heat shock response. {ECO:0000250|UniProtKB:P0DMV8}.
-!- SUBUNIT: Component of the CatSper complex. Identified in a IGF2BP1-
dependent mRNP granule complex containing untranslated mRNAs. Interacts
with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the
interaction occurs in the absence of the RNA component, TERC, and
dissociates once the TERT complex has formed. Interacts with METTL21A.
Interacts with DNAAF2. Interacts with TRIM5 (via B30.2/SPRY domain).
Interacts with PRKN. Interacts with FOXP3. Interacts with NOD2; the
interaction enhances NOD2 stability. Interacts with DNAJC9 (via J
domain). Interacts with ATF5; the interaction protects ATF5 from
degradation via proteasome-dependent and caspase-dependent processes.
Interacts with RNF207 (via the C-terminus); this interaction additively
increases KCNH2 expression. Interacts with HSF1 (via transactivation
domain); this interaction results in the inhibition of heat shock- and
HSF1-induced transcriptional activity during the attenuation and
recovery phase period of the heat shock response. Interacts with NAA10,
HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form
interact with HOPX and STUB1 respectively. Interacts with NEDD1 and
SMAD3. Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105.
Interacts with DNAJC8. Interacts with NLRP12. Interacts with PGLYRP.
{ECO:0000250|UniProtKB:P0DMV8, ECO:0000250|UniProtKB:Q61696}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV8}. Nucleus
{ECO:0000250|UniProtKB:P0DMV8}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV8}. Secreted
{ECO:0000250|UniProtKB:Q61696}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV8}.
-!- INDUCTION: By heat shock.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
the ATPase domain) is responsible for binding and hydrolyzing ATP. The
C-terminal substrate-binding domain (SBD) (also known as peptide-
binding domain) binds to the client/substrate proteins. The two domains
are allosterically coupled so that, when ATP is bound to the NBD, the
SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
conformational change enhances the affinity of the SBD for client
proteins. {ECO:0000250|UniProtKB:P0DMV8}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P0DMV8}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; X77208; CAA54423.1; -; Genomic_DNA.
EMBL; BX883045; CAE83978.1; -; Genomic_DNA.
PIR; I54542; I54542.
RefSeq; NP_114177.2; NM_031971.2.
RefSeq; NP_997669.1; NM_212504.1.
RefSeq; XP_017457331.1; XM_017601842.1.
SMR; P0DMW0; -.
CORUM; P0DMW0; -.
STRING; 10116.ENSRNOP00000067749; -.
CarbonylDB; P0DMW0; -.
iPTMnet; P0DMW0; -.
jPOST; P0DMW0; -.
PaxDb; P0DMW0; -.
PRIDE; P0DMW0; -.
DNASU; 24472; -.
Ensembl; ENSRNOT00000049667; ENSRNOP00000050605; ENSRNOG00000045654.
Ensembl; ENSRNOT00000061950; ENSRNOP00000067749; ENSRNOG00000045654.
Ensembl; ENSRNOT00000081924; ENSRNOP00000075599; ENSRNOG00000050647.
GeneID; 108348108; -.
GeneID; 24472; -.
GeneID; 294254; -.
KEGG; rno:24472; -.
CTD; 3303; -.
CTD; 3304; -.
RGD; 1593284; Hspa1a.
eggNOG; KOG0101; Eukaryota.
OMA; HIEVEYK; -.
OrthoDB; 288077at2759; -.
PhylomeDB; P0DMW0; -.
Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-RNO-3371568; Attenuation phase.
Reactome; R-RNO-3371571; HSF1-dependent transactivation.
Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P0DMW0; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000045654; Expressed in esophagus and 19 other tissues.
ExpressionAtlas; P0DMW0; baseline and differential.
GO; GO:0016235; C:aggresome; ISO:RGD.
GO; GO:0005814; C:centriole; ISO:RGD.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016234; C:inclusion body; ISO:RGD.
GO; GO:0045121; C:membrane raft; IDA:CAFA.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032991; C:protein-containing complex; ISO:RGD.
GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
GO; GO:0005524; F:ATP binding; ISO:RGD.
GO; GO:0016887; F:ATPase activity; ISO:RGD.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:RGD.
GO; GO:0031249; F:denatured protein binding; ISO:RGD.
GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
GO; GO:0070370; P:cellular heat acclimation; ISO:RGD.
GO; GO:0034605; P:cellular response to heat; ISO:RGD.
GO; GO:0034620; P:cellular response to unfolded protein; ISO:RGD.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:RGD.
GO; GO:0006281; P:DNA repair; ISO:RGD.
GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:RGD.
GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:RGD.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:1902380; P:positive regulation of endoribonuclease activity; ISO:RGD.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:RGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:0033120; P:positive regulation of RNA splicing; ISO:RGD.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
GO; GO:0006457; P:protein folding; ISO:RGD.
GO; GO:0042026; P:protein refolding; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:RGD.
GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009408; P:response to heat; ISO:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0006986; P:response to unfolded protein; IMP:RGD.
GO; GO:0000723; P:telomere maintenance; ISO:RGD.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR043129; ATPase_NBD.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
SUPFAM; SSF53067; SSF53067; 2.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Secreted;
Stress response.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
CHAIN 2..641
/note="Heat shock 70 kDa protein 1A"
/id="PRO_0000078254"
NP_BIND 12..15
/note="ATP"
/evidence="ECO:0000250"
NP_BIND 202..204
/note="ATP"
/evidence="ECO:0000250"
NP_BIND 268..275
/note="ATP"
/evidence="ECO:0000250"
NP_BIND 339..342
/note="ATP"
/evidence="ECO:0000250"
REGION 2..386
/note="Nucleotide-binding domain (NBD)"
/evidence="ECO:0000250|UniProtKB:P11142"
REGION 394..509
/note="Substrate-binding domain (SBD)"
/evidence="ECO:0000250|UniProtKB:P11142"
REGION 618..641
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
BINDING 71
/note="ATP"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 77
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 108
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 246
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 348
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 469
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 561
/note="N6,N6,N6-trimethyllysine; by METTL21A; alternate"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 561
/note="N6,N6-dimethyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 631
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 633
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
MOD_RES 636
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P0DMV8"
SEQUENCE 641 AA; 70185 MW; 2D745B1013F64E7B CRC64;
MAKKTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVVNDGDK PKVQVNYKGE NRSFYPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRERVAAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDSNTLAEKE EFVHKREELE
RVCNPIISGL YQGAGAPGAG GFGAQAPKGG SGSGPTIEEV D


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Pathways :
WP2199: Seed Development
WP1502: Mitochondrial biogenesis
WP1049: G Protein Signaling Pathways
WP1692: Protein export
WP931: G Protein Signaling Pathways
WP1650: Fluorobenzoate degradation
WP2203: TSLP Signaling Pathway
WP1659: Glycine, serine and threonine metabolism
WP2292: Chemokine signaling pathway
WP1199: Apoptosis Modulation by HSP70
WP1700: Selenoamino acid metabolism
WP1438: Influenza A virus infection
WP1888: Post-translational protein modification
WP1663: Homologous recombination
WP2371: Parkinsons Disease Pathway
WP1673: Naphthalene and anthracene degradation
WP384: Apoptosis Modulation by HSP70
WP1531: Vitamin D synthesis
WP1909: Signal regulatory protein (SIRP) family interactions
WP1616: ABC transporters
WP2032: TSH signaling pathway
WP1678: Nucleotide excision repair
WP73: G Protein Signaling Pathways
WP1690: Propanoate metabolism
WP843: Apoptosis Modulation by HSP70

Related Genes :
[Hspa1a Hsp70-1 Hspa1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[HSPA1A HSP72 HSPA1 HSX70] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[Hspa1a Hsp70-3 Hsp70A1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 3) (HSP70.3) (Hsp68)
[HSPA1A HSP70-1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70.1)
[HSP70-4 HSC70-4 HSP70 MED37_2 MED37C At3g12580 T16H11.7 T2E22.11] Heat shock 70 kDa protein 4 (Heat shock cognate 70 kDa protein 4) (Heat shock cognate protein 70-4) (AtHsc70-4) (Heat shock protein 70-4) (AtHsp70-4)
[Hspa1b Hsp70-2 Hspa2] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1)
[HSPA1B HSP72] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
[Hspa1b Hcp70.1 Hsp70-1 Hsp70a1 Hspa1] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 1) (HSP70.1)
[HSPA1A HSPA1] Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70.1)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Steroidogenesis-activator polypeptide)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Fragment)
[HSPA5 GRP78 I79_019946] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPBP1 HSPBP PP1845] Hsp70-binding protein 1 (HspBP1) (Heat shock protein-binding protein 1) (Hsp70-binding protein 2) (HspBP2) (Hsp70-interacting protein 1) (Hsp70-interacting protein 2)
[HSPA1B HSP70-2] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70.2)
[HSPA9 GRP75 HSPA9B mt-HSP70] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[SSB1 YG101 YDL229W] Ribosome-associated molecular chaperone SSB1 (EC 3.6.4.10) (Cold-inducible protein YG101) (Heat shock protein SSB1) (Hsp70 chaperone Ssb)
[HSPA14 HSP60 HSP70L1] Heat shock 70 kDa protein 14 (HSP70-like protein 1) (Heat shock protein HSP60)
[SSB2 YG103 YNL209W N1333] Ribosome-associated molecular chaperone SSB2 (EC 3.6.4.10) (Heat shock protein SSB2) (Hsp70 chaperone Ssb)
[HSPA1B] Heat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70.2)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA1 Hsp70] Heat shock 70 kDa protein 1
[Hspa8 Hsc70 Hsc73] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8)
[HSPA8 HSC70 HSP73 HSPA10] Heat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)
[Hspa9 Grp75 Hsp74 Hspa9a] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)

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