HSP70-1A (HSPA1A) Rabbit Polyclonal Antibody

CAT#: AP31742PU-N

HSP70-1A (HSPA1A) rabbit polyclonal antibody, Aff - Purified

Product Images

Human Testis: Formalin-Fixed, Paraffin-Embedded (FFPE)

Specifications

Product Data

• Applications: IHC, WB
• Recommended Dilution: Immunohistochemistry on Paraffin Sections: 2 µg/ml.
  Western Blot.
• Reactivities: Human
• Host: Rabbit
• Isotype: IgG
• Clonality: Polyclonal
• Immunogen: Synthetic peptide
• Specificity: Recognizes HSP70
• Formulation: PBS, pH 7.4 containing 0.02% Sodium Azide as preservative
  State: Aff - Purified
  State: Liquid purified Ig fraction
• Concentration: lot specific
• Purification: Affinity Chromatography
• Storage: Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
  Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.
• Gene Name: Homo sapiens heat shock protein family A (Hsp70) member 1A (HSPA1A)
• Database Link:
  Entrez Gene 3303 Human
• Background: Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eucaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eucaryotes 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 (2). 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 (3). 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 (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5).
  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 (6). 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: HSP70.1, HSP70-1/HSP70-2, HSPA1A, HSPA1B, HSPA1

Reference Data

• Protein Pathways: Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Prion diseases, Spliceosome