SKU: WP2270 Categories: ,

BAG2 Polyclonal Antibody

Price range: $268.00 through $328.00

SKU: WP2270-100
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Product details

Background:

BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008],

Specifications

Size50μL/100μL
TargetBAG2
ReactivityHuman, Mouse
ApplicationsWB, ELISA
MW(Calculated)
MW(Observed)23kD
Host SpeciesRabbit
IsotypeIgG
Conjugate/ModificationUnmodified
Recommended Dilution RatioWB 1:500-2000; ELISA 1:5000-20000
FormulationLiquid in PBS containing 50% glycerol,0.5% BSA and 0.02% sodium azide.
PurificationThe antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Storage-15°C to -25°C/1 year(Do not lower than -25°C)
Concentration1 mg/ml
ClonalityPolyclonal
Clone Number
ImmunogenSynthesized peptide derived from part region of human protein
SpecificityBAG2 Polyclonal Antibody detects endogenous levels of protein.
Gene NameBAG2
Protein NameBAG family molecular chaperone regulator 2 (BAG-2) (Bcl-2-associated athanogene 2)
Other Name
SpeciesHuman
Gene ID9532
UniprotO95816,
Species.1Mouse
Gene ID.1
Uniprot.1Q91YN9
Species.2
Gene ID.2
Uniprot.2
Cellular Localizationcytosol,
Tissue ExpressionUterus,
Signaling_pathwayGenetic Information Processing >> Folding, sorting and degradation >> Protein processing in endoplasmic reticulum
Research Areas>>Protein processing in endoplasmic reticulum
FunctionFunction:Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.,similarity:Contains 1 BAG domain.,subunit:Binds to the ATPase domain of HSP70/HSC chaperones.,
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