Alternative Name: | HspA1A, Heat shock protein 70, HspA1B |
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Clone: | C92F3A-5 |
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Host: | Mouse |
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Isotype: | IgG1 |
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Immunogen: | Native human Hsp70. |
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UniProt ID: | P0DMV8 (HSPA1A), P0DMV9 (HSPA1B) |
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GenBank ID: | M11717 |
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Gene/Protein Identifier: | NP_005336.3 (RefSeq), NM_005345 (RefSeq), 3303 (Entrez GeneID), 140550 (OMIM) |
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Source: | Purified from hybridoma tissue culture supernatant. |
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Species reactivity: | Human, Mouse, Rat Bovine, Chicken, Dog, Drosophila, Fish, Guinea pig, Hamster, Monkey, Porcine, Rabbit, Sheep
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Applications: | Flow Cytometry
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Recommended Dilutions/Conditions: | Flow Cytometry (1:20- 1:100)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application. |
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Application Notes: | Detects a band of ~70kDa by Western blot. |
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Purity Detail: | Protein G affinity purified. |
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Formulation: | Liquid. In PBS, pH 7.2, containing 0.09% sodium azide. |
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Handling: | Avoid freeze/thaw cycles. Protect from light. |
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Shipping: | Blue Ice Not Frozen |
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Long Term Storage: | +4°C |
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Scientific Background: | The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway. |
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Regulatory Status: | RUO - Research Use Only |
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