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Home Antibody All anti-HSPA1A antibodies

Anti-HSPA1A Antibody 3A3

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Specifications Citations Related Products Product Documents
SKU Description Amount Price Availability*  
TA326360
  • Mouse monoclonal Hsp70 Antibody
  • FREE positive control: HEK293T cell transient overexpression lysate (LC401646) , 20ug
100µg 325 3-7 Days
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Also for HSPA1A (NM_005345)
cDNA Clone shRNA/siRNA Lysate Protein Antibody

OriGene Data

ImmunogenHuman Recombinant Hsp70 overexpressed in E.coli
Clone Name3A3 IsotypeIgG1
Species ReactivityHuman, Mouse, Rat, Amphibian, Chicken, Fish, Saccharomyces cerevisiae, Fruit Fly Concentration1mg/mL
Guaranteed Application *WB Suggested DilutionsICC: 1:500, WB: 1:5000; IP: 1-2ug
BufferPBS pH7.2, 50% glycerol, 0.09% sodium azide
Purification Protein G Purified
Note Detects several members of the heat shock protein 70kDa gene family including Hsp70, Hsc70, p75 and following heat shock, Hsp72 from yeast, Drosophila, fish, mouse, avian, amphibian and human samples.

Reference Data

Target NameHomo sapiens heat shock 70kDa protein 1A (HSPA1A)
Alternative NameHEL-S-103; HSP70-1; HSP70-1A; HSP70I; HSP72; HSPA1
Database LinkNP_005336
FunctionHsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity . The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides . When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half . The structure of this ATP binding domain displays multiple features of nucleotide binding proteins . All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein . The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.
Related Pathway
MAPK signaling pathway

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10ug cell free extract from Artemia probed with anti-Hsp70

 

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