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Home Antibody All anti-Git1 antibodies

Anti-Git1 Antibody S39B-8

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SKU Description Amount Price Availability*  
TA326533
  • Mouse Monoclonal Anti-GIT1 Antibody
100µg $325 3-7 Days
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OriGene Data

ImmunogenFusion protein amino acids 375-770 (C-terminus) of Rat GIT1
Clone NameS39B-8 IsotypeIgG1
Species ReactivityHuman, Mouse, Rat Concentration1mg/mL
Guaranteed Application * Suggested Dilutions
BufferPBS pH7.4, 50% glycerol
Purification Protein G Purified
Note ~90kDa. Does not cross-react

Reference Data

Target NameRattus norvegicus G protein-coupled receptor kinase interacting ArfGAP 1 (Git1)
Alternative Name
Database LinkNP_114002
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 Cterminal 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.
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