HSP70 1A Protein (His tag)
Quick Overview for HSP70 1A Protein (His tag) (ABIN7317034)
Target
See all HSP70 1A (HSPA1A) ProteinsProtein Type
Biological Activity
Origin
Source
Purity
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Purification tag / Conjugate
- This HSP70 1A protein is labelled with His tag.
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Purpose
- Recombinant Human HSP70/HSPA1A Protein (His Tag)(Active)
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Sequence
- Ala 2-Asp 641
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Characteristics
- A DNA sequence encoding the human HSPA1A (NP_005337.2) (Ala2-Asp641) was expressed, with a polyhistidine tag at the N-terminus.
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Endotoxin Level
- < 1.0 EU per μg as determined by the LAL method.
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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
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Format
- Lyophilized
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Reconstitution
- Please refer to the printed manual for detailed information.
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Buffer
- Lyophilized from sterile 20 mM Tris, 500 mM NaCl, pH 7.4, 10 % glycerol
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Storage
- 4 °C,-20 °C,-80 °C
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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.
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- HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))
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Alternative Name
- HSP70/HSPA1A
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Background
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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
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Molecular Weight
- 72.2 kDa
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UniProt
- P08107
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Pathways
- Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process
Target
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