Hsc70 antibody (N-Term)
Quick Overview for Hsc70 antibody (N-Term) (ABIN3044300)
Target
See all Hsc70 (HSPA8) AntibodiesReactivity
Host
Clonality
Conjugate
Application
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Binding Specificity
- N-Term
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Purpose
- Anti-Hsp70/HSPA1A/HSPA1B Antibody
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Sequence
- TTYSCVGVFQ HGKVEIIAN
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Specificity
- No cross reactivity with other proteins.
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Cross-Reactivity (Details)
- No cross-reactivity with other proteins
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Predicted Reactivity
- identical to the related rat,mouse sequence.
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Characteristics
- Anti-Hsp70/HSPA1A/HSPA1B Antibody. Tested in Flow Cytometry, IF, IHC, IHC-F, ICC, WB applications. This antibody reacts with Human, Mouse, Rat.
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Purification
- Immunogen affinity purified.
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Immunogen
- A synthetic peptide corresponding to a sequence at the N-terminus of human Hsp70, identical to the related rat and mouse sequence.
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Isotype
- IgG
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Application Notes
- Western blot, 0.1-0.5 μg/mL, Human, Mouse, Rat Immunohistochemistry (Paraffin-embedded Section), 0.5-1 μg/mL, Human, Mouse, Rat Immunohistochemistry (Frozen Section), 0.5-1 μg/mL, Mouse, Rat Immunocytochemistry , 0.5-1 μg/mL, Human Immunocytochemistry/Immunofluorescence, 2 μg/mL, Human Flow Cytometry (Fixed), 1-3 μg/1x106 cells, Human
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Comment
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Antibody can be supported by chemiluminescence kit ABIN921124 in WB, supported by ABIN921231 in IHC(P), IHC(F) and ICC.
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Reconstitution
- Add 0.2 mL of distilled water will yield a concentration of 500 μg/mL.
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Concentration
- 500 μg/mL
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Buffer
- Each vial contains antibody formulated with stabilizing components, 0.9 mg NaCl, 0.2 mg Na2HPO4, 0.05 mg Thimerosal, 0.05 mg Sodium azide.
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Preservative
- Thimerosal (Merthiolate), Sodium azide
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Precaution of Use
- This product contains Thimerosal (Merthiolate) and Sodium azide: POISONOUS AND HAZARDOUS SUBSTANCES which should be handled by trained staff only.
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Handling Advice
- Avoid repeated freezing and thawing.
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Storage
- 4 °C,-20 °C
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Storage Comment
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Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month.
It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles. -
Expiry Date
- 12 months
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: "Effects of intracerebral hemorrhage and subsequent minimally invasive hematoma aspiration on expression of apoptosisrelated genes in rats." in: International journal of clinical and experimental pathology, Vol. 8, Issue 5, pp. 5371-8, (2016) (PubMed).
: "Effects of minocycline on the expression of NGF and HSP70 and its neuroprotection role following intracerebral hemorrhage in rats." in: Journal of biomedical research, Vol. 25, Issue 4, pp. 292-8, (2013) (PubMed).
: "Therapeutic efficacy of trehalose eye drops for treatment of murine dry eye induced by an intelligently controlled environmental system." in: Molecular vision, Vol. 18, pp. 317-29, (2012) (PubMed).
: "Effect of pre-moxibustion on apoptosis and proliferation of gastric mucosa cells." in: World journal of gastroenterology, Vol. 13, Issue 15, pp. 2174-8, (2007) (PubMed).
: "Down-modulation of heat shock protein 70 and up-modulation of Caspase-3 during schisandrin B-induced apoptosis in human hepatoma SMMC-7721 cells." in: World journal of gastroenterology, Vol. 10, Issue 20, pp. 2944-8, (2004) (PubMed).
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- Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
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Alternative Name
- HSPA8
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Background
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Background: The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. All of the Hsp70 proteins have three major functional domains: An N-terminal ATPase domain binds ATP (Adenosine triphosphate) and hydrolyzes it to ADP (Adenosine diphosphate); A substrate binding domain contains a groove with an affinity for neutral, hydrophobic amino acid residues; A C-terminal domain rich in alpha helical structure acts as a 'lid' for the substrate binding domain. By binding tightly to partially-synthesized peptide sequences (incomplete proteins), Hsp70 prevents them from aggregating and being rendered nonfunctional. And it also can act to protect cells from thermal or oxidative stress. Finally, Hsp70 seems to be able to participate in disposal of damaged or defective proteins. Interaction with CHIP (Carboxyl-terminus of Hsp70 Interacting Protein)–an E3 ubiquitin ligase–allows Hsp70 to pass proteins to the cell's ubiquitination and proteolysis pathways.
Gene Full Name: heat shock protein family A (Hsp70) member 1A/1B
Sequence Similarities: Belongs to the beta-catenin family.
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Molecular Weight
- 70 kDa
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Gene ID
- 3303, 3304
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UniProt
- P0DMV8
Target
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