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Anti-HSP70 antibody

[STJ96944] Download PDF Print Data Sheet

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Product name Anti-HSP70 antibody
Short Description Mouse Monoclonal to HSP70.
Description HSP70 is encoded by the HSPA gene family which includes many variants of the gene. It is approximately 70kDa. There are numerous members of the HSP70 heat shock protein. HSP70 is localised to the cytoplasm. It colocalizes with SHCBP1L at spindle during the meiosis process. HSP70 is a molecular chaperone that is implicated in a wide variety of cellular processes such as the 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. It is also considered a cellular thermometer in response to heat stress and other stimuli. HSP70 is expressed in nearly every cellular compartment in eukaryotes. Mutations in the HSPA gene result in protein folding disorders, autoimmune diseases and cancer. STJ96944 was developed from clone 3G10. The antibody was affinity-purified from mouse ascites by affinity-chromatography using specific immunogen. This primary antibody binds endogenous HSP70.
Applications IF, WB
Dilution range WB 1:1000-2000 / IF 1:100-200
Specificity The antibody detects endogenous HSP70 proteins.
Protein Name Heat shock 70 kDa protein 1-like/Heat shock 70 kDa protein 1A/1B - HSPA1L - HSP70-HOM - hum70t - heat shock protein family A (Hsp70) member 1 like
Immunogen Synthetic Peptide
Storage Instruction Store at -20°C, and avoid repeat freeze-thaw cycles.
Note For Research Use Only (RUO).
Host Mouse
Clonality Monoclonal
Clone ID 3G10
Reactivity Human, Mouse, Rat
Conjugation Unconjugated
Purification The antibody was affinity-purified from mouse ascites by affinity-chromatography using specific immunogen.
Isotype IgG1
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene ID 3305/3303/3304 (Human) / 15482/193740 (Mouse) / 24963/24472 (Rat)
Gene Symbol HSPA1L
Database Links Human UniProt/Swiss-Prot:P34931 Human Entrez Gene: 3305
Alternative Names HSPA1L / heat shock protein family A (Hsp70) member 1 like / D623_10007240 antibody / heat shock 10kDa protein 1-like antibody / heat shock 70 kDa-like protein 1 antibody / Heat shock 70 kDa protein 1 antibody / heat shock 70 kDa protein 1-Hom antibody / Heat shock 70 kDa protein 1L antibody / heat shock 70 kDa protein 1-like antibody / heat shock 70kDa protein 1-like antibody / Heat shock 70 kDa protein 1-like protein antibody / heat shock 70 kDa protein 3 antibody / heat shock 70kD protein-like 1 antibody / heat shock cognate protein 70 antibody / heat shock protein 1-like antibody / heat shock protein 70 1L antibody / Heat shock protein 70-1l antibody / heat shock protein cognate 70 / testis antibody / heat shock-related protein hsc70t antibody / hsc70 antibody / hsc70.I antibody / Hsc70t antibody / hsp70 antibody / HSP70-1L antibody / Hsp70-3 antibody / HSP70.3 antibody / HSP70-HOM antibody / HSP70T antibody / hum70t antibody / inducible heat shock protein 70 antibody / Msh5 antibody / PANDA_021870 antibody / QtsA-15024 antibody / spermatid-specific heat shock protein 70 antibody / TREES_T100017790 antibody
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 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 . Positive regulator of PRKN translocation to damaged mitochondria .
Tissue Specificity Expressed in spermatids.
Sequence and Domain Family 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.

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