HSP70-1A (HSPA1A) Mouse Monoclonal Antibody [Clone ID: N27F3-4]

Specifications

Product Data
Clone Name	N27F3-4
Applications	WB
Recommend Dilution	1ug/ml was sufficient for detection of hsp/hsc70 in 20ug of HeLa lysate.
Reactivity	Human, Mouse, Rat, Bovine, Canine, Chicken, Drosophila, Fish, Monkey, Pig, Plant, Rabbit, Sheep, Xenopus, Beluga, Hamster, Guinea Pig, C. elegans
Host	Mouse
Clonality	Monoclonal
Immunogen	Recombinant Hsp70/hsc70
Formulation	PBS pH7.2, 50% glycerol, 0.09% sodium azide
Concentration	lot specific
Purification	Protein G Purified
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Gene Name	heat shock protein family A (Hsp70) member 1A
Database Link	NP_005336 Entrez Gene 24472 RatEntrez Gene 193740 MouseEntrez Gene 3303 Human UniProt ID P0DMV8
Background	Hsp70 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.
Synonyms	HEL-S-103; HSP70-1; HSP70-1A; HSP70.1; HSP70I; HSP72; HSPA1
Note	Detects 72 and 73kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots.
Reference Data
Protein Pathways	Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Prion diseases, Spliceosome

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