PRODUCT CODE: ER50802

HSP70 Antibody (ER50802)

Applications

  • WB

  • ICC

  • IHC-P

REACTIVITY

  • Human

  • Mouse

  • Rat

  • Cow

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Western blot analysis of HSP70 on different cell lysates using anti-HSP70 antibody at 1/500 dilution.<br />
 Positive control: <br />
 Lane 1: A549 <br />
 Lane 2: MCF-7 <br />
 Lane 3: HCT116
  • Western blot analysis of HSP70 on different cell lysates using anti-HSP70 antibody at 1/500 dilution.<br />
 Positive control: <br />
 Lane 1: A549 <br />
 Lane 2: MCF-7 <br />
 Lane 3: HCT116
  • ICC staining HSP70 in SHG-44 cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
  • ICC staining HSP70 in A431 cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
  • ICC staining HSP70 in SKBR-3 cells (green). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
  • Immunohistochemical analysis of paraffin-embedded human breast cancer tissue using anti-HSP70 antibody. Counter stained with hematoxylin.
  • Immunohistochemical analysis of paraffin-embedded mouse testis tissue using anti-HSP70 antibody. Counter stained with hematoxylin.
  • Immunohistochemical analysis of paraffin-embedded mouse brain tissue using anti-HSP70 antibody. Counter stained with hematoxylin.
  • Immunohistochemical analysis of paraffin-embedded mouse prostate tissue using anti-HSP70 antibody. Counter stained with hematoxylin.
Western blot analysis of HSP70 on different cell lysates using anti-HSP70 antibody at 1/500 dilution.
Positive control:
Lane 1: A549
Lane 2: MCF-7
Lane 3: HCT116

Applications

  • WB

  • ICC

  • IHC-P

REACTIVITY

  • Human

  • Mouse

  • Rat

  • Cow

SPECIFICATIONS

Product Type

Rabbit polyclonal primary

Product Name

HSP70 Antibody (ER50802)

Immunogen

Synthetic peptide within human hsp70 aa 10-50.

Host

Rabbit

Positive Control

A549, MCF-7, HCT116, A431, SHG-44, SKBR-3, mouse testis tissue, mouse prostate tissue, mouse brain tissue, human breast cancer tissue.

Conjugation

Unconjugated

Clonality

Polyclonal

PROPERTIES

Form

Liquid

Storage Condition

Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.

Storage Buffer

1*PBS (pH7.4), 0.2% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.

Concentration

1 ug/ul

PURIFICATION

Peptide affinity purified

MOLECULAR WEIGHT

70 kDa

Isotype

IgG

APPLICATION DILUTION

  • WB

  • 1:500

  • ICC

  • 1:200

  • IHC-P

  • 1:200

TARGET

UNIPROT #

PROTEIN NAME

HSP70

SYNONYMS

DnaK type molecular chaperone HSP70 1 antibody; Epididymis secretory protein Li 103 antibody; FLJ54303 antibody; FLJ54370 antibody; FLJ54392 antibody; FLJ54408 antibody; FLJ75127 antibody; Heat shock 70 kDa protein 1 antibody; Heat shock 70 kDa protein 1/2 antibody; Heat shock 70 kDa protein 1A/1B antibody; Heat shock 70kDa protein 1A antibody; Heat shock 70kDa protein 1B antibody; Heat shock induced protein antibody; HEL S 103 antibody; HSP70 1 antibody; HSP70 1B antibody; HSP70 2 antibody; HSP70-1/HSP70-2 antibody; HSP70-1A antibody; HSP70.1 antibody; HSP70.1/HSP70.2 antibody; HSP70I antibody; HSP71_HUMAN antibody; HSP72 antibody; HSPA1 antibody; HSPA1A antibody; HSPA1B antibody

SEQUENCE SIMILARITIES

Belongs to the heat shock protein 70 family.

POST-TRANSLATIONAL MODIFICATION

In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.

SUBCELLULAR LOCATION

Cytoplasm.

FUNCTION

The 70 kilodalton heat shock proteins (Hsp70s) are a family of conserved ubiquitously expressedheat shock proteins. Proteins with similar structure exist in virtually all living organisms. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. When not interacting with a substrate peptide, Hsp70 is usually in an ATP bound state. Hsp70 by itself is characterized by a very weak ATPase activity, such that spontaneous hydrolysis will not occur for many minutes. As newly synthesized proteins emerge from the?ribosomes, the substrate binding domain of Hsp70 recognizes sequences of hydrophobic amino acid residues, and interacts with them. This spontaneous interaction is reversible, and in the ATP bound state Hsp70 may relatively freely bind and release peptides. However, the presence of a peptide in the binding domain stimulates the ATPase activity of Hsp70, increasing its normally slow rate of ATP hydrolysis.