HSP70 1A antibody
Quick Overview for HSP70 1A antibody (ABIN7540521)
Target
See all HSP70 1A (HSPA1A) AntibodiesReactivity
Host
Clonality
Conjugate
Application
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Supplier Product No.
- 200-901-f63
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Supplier
- Rockland
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Purpose
- Hsp70 Antibody
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Cross-Reactivity (Details)
- A BLAST analysis was used to suggest cross-reactivity with Hsp70 from Human, Rat, and Mouse based on 100 % homology with the immunizing sequence.
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Purification
- Anti-Hsp70 Antibody was prepared from IgY and PEG purified.
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Sterility
- Sterile filtered
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Immunogen
- Hsp70 Antibody was produced in chicken prepared by repeated immunizations raised against full length protein Hsp70.
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Isotype
- IgG
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Application Notes
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ELISA_Dilution: 1:200
Western_Blot_Dilution: 1:1000
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Comment
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Anti-Hsp70 Antibody is tested for use in WB and IF. Specific conditions for reactivity should be optimized by the end user.
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Restrictions
- For Research Use only
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Format
- Liquid
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Buffer
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Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Stabilizer: 50 % (v/v) Glycerol
Preservative: 0.1 % (w/v) Sodium Azide -
Preservative
- Sodium azide
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Precaution of Use
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Storage
- 4 °C,-20 °C
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Storage Comment
- Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
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Expiry Date
- 12 months
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- HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))
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Alternative Name
- HSPA1A
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Background
- Heat shock 70 kDa protein, HSP70,Hsp70 genes encode abundant heat-inducible 70- kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes 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 50 % identity. 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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. 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.
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Gene ID
- 3303
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NCBI Accession
- NP_005336
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UniProt
- P0DMV8
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Pathways
- Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process
Target
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