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HSP70 1A Protein (His tag)

This Recombinant HSP70 1A protein is produced in Baculovirus infected Insect Cells.
Catalog No. ABIN7317034

Quick Overview for HSP70 1A Protein (His tag) (ABIN7317034)

Target

See all HSP70 1A (HSPA1A) Proteins
HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 6
  • 3
  • 2
  • 2
  • 2
Human

Source

  • 14
  • 1
Baculovirus infected Insect Cells

Purity

> 85 % as determined by reducing SDS-PAGE.
  • Purification tag / Conjugate

    This HSP70 1A protein is labelled with His tag.

    Purpose

    Recombinant Human HSP70/HSPA1A Protein (His Tag)(Active)

    Sequence

    Ala 2-Asp 641

    Characteristics

    A DNA sequence encoding the human HSPA1A (NP_005337.2) (Ala2-Asp641) was expressed, with a polyhistidine tag at the N-terminus.

    Endotoxin Level

    < 1.0 EU per μg as determined by the LAL method.

    Biological Activity Comment

    1. Measured by its ability to bind human PARP1 in a functional ELISA.2. Measured by its ability to bind mouse PARP1 in a functional ELISA.
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  • Restrictions

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    Please refer to the printed manual for detailed information.

    Buffer

    Lyophilized from sterile 20 mM Tris, 500 mM NaCl, pH 7.4, 10 % glycerol

    Storage

    4 °C,-20 °C,-80 °C

    Storage Comment

    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target

    HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))

    Alternative Name

    HSP70/HSPA1A

    Background

    Background: HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP are synthesized intracellularly, which may protect cells from protein denaturation or from death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release. 

    Synonym: HEL-S-103;HSP70-1;HSP70-1A;HSP70I;HSP72;HSPA1

    Molecular Weight

    72.2 kDa

    UniProt

    P08107

    Pathways

    Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process
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