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Anti-HSP60 Antibody [9-49]

M1007-9
HUABIO
ApplicationsFlow Cytometry, ImmunoFluorescence, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Mouse, Rat
TargetHSPD1
100 ul
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Overview

  • Supplier
    HUABIO
  • Product Name
    Anti-HSP60 Antibody [9-49]
  • Delivery Days Customer
    7
  • Applications
    Flow Cytometry, ImmunoFluorescence, Western Blot, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
  • Applications Supplier
    WB,IF-Cell,IHC-P,FC
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    9-49
  • Concentration
    2 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID3329
  • Target name
    HSPD1
  • Target description
    heat shock protein family D (Hsp60) member 1
  • Target synonyms
    CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, 60 kDa heat shock protein, mitochondrial, 60 kDa chaperonin, P60 lymphocyte protein, chaperonin 60, epididymis secretory sperm binding protein, heat shock 60kDa protein 1 (chaperonin), heat shock protein 65, heat shock protein family D member 1, mitochondrial matrix protein P1, short heat shock protein 60 Hsp60s1
  • Host
    Mouse
  • Isotype
    IgG2a
  • Protein IDP10809
  • Protein Name
    60 kDa heat shock protein, mitochondrial
  • Scientific Description
    HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional tertiary structure. The energy to fold proteins is supplied by non-covalent interactions between the amino acid side chains of each protein, and by solvent effects. Most proteins spontaneously fold into their most stable three-dimensional conformation, which is usually also their functional conformation, but occasionally proteins mis-fold. Molecular chaperones catalyze protein refolding by accelerating partial unfolding of misfolded proteins, aided by energy supplied by the hydrolysis of adenosine triphosphate (ATP). Chaperonin proteins may also tag misfolded proteins to be degraded.
  • Reactivity
    Human, Mouse, Rat
  • Reactivity Supplier
    Human,Mouse,Rat
  • Storage Instruction
    -20°C,2°C to 8°C
  • UNSPSC
    41116161