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HSP70 (D1M6J) Mouse mAb (BSA and Azide Free)

HSP70 (D1M6J) Mouse mAb (BSA and Azide Free) #24348

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)	70
Source/Isotype	Mouse IgG1

Application Key:

WB-Western Blotting
IHC-Immunohistochemistry

Species Cross-Reactivity Key:

H-Human

Product Information

Product Usage Information

This product is the carrier free version of product #46477. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

Formulation

Supplied in 1X PBS (10 mM Na₂HPO₄, 3 mM KCl, 2 mM KH₂PO₄, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

For standard formulation of this product see product #46477

Storage

Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

Specificity / Sensitivity

HSP70 (D1M6J) Mouse mAb (BSA and Azide Free) recognizes endogenous levels of total HSP70 protein. This antibody does not cross-react with Heat shock-related 70 kDa protein 2 (HSPA2) or Heat shock cognate 71 kDa protein (HSC70/HSPA8).

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg72 of human HSP70 protein (HSPA1A/HSPA1B).

Background

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

Database Links

UniProt ID: P0DMV8

Entrez-Gene Id: 3303

Limited Uses

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For Research Use Only. Not For Use In Diagnostic Procedures.

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