Recombinant Rat HSPA1A Protein, His (Fc)-Avi-tagged
Cat.No. : | HSPA1A-2599R |
Product Overview : | Recombinant Rat HSPA1A with His (Fc)-Avi tag was expressed and purified |
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Source : | HEK293 |
Species : | Rat |
Tag : | His&Fc&Avi |
Endotoxin : | < 1.0 EU per μg of the protein as determined by the LAL method |
Purity : | ≥85% by SDS-PAGE |
Stability : | Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : | For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles. |
Storage Buffer : | PBS buffer |
Gene Name : | Hspa1a heat shock 70kD protein 1A [ Rattus norvegicus ] |
Official Symbol : | HSPA1A |
Gene ID : | 24472 |
mRNA Refseq : | NM_031971.2 |
Protein Refseq : | NP_114177.2 |
UniProt ID : | Q07439 |
Products Types
◆ Recombinant Protein | ||
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HSPA1A-0702H | Recombinant Human HSPA1A Protein (M1-D641), His/Strep tagged | +Inquiry |
HSPA1A-2622H | Recombinant Human HSPA1A protein(351-600 aa), C-His-tagged | +Inquiry |
Hspa1a-1638R | Recombinant Rat Hspa1a Protein, His-tagged | +Inquiry |
HSPA1A-1117H | Recombinant Human HSPA1A Protein, His (Fc)-Avi-tagged | +Inquiry |
◆ Lysates | ||
HSPA1A-519HCL | Recombinant Human HSPA1A cell lysate | +Inquiry |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewUsing HSPA1A experiments can obtain consistent results and reduce the uncertainty of experiments.
HSPA1A has good stability and is suitable for long-term storage and use.
HSPA1A can effectively simulate the function of the target protein in vitro.
Q&As (6)
Ask a questionHSPA1A has multiple associations with other proteins and diseases. For example, it may interact with the p53 protein to affect the occurrence and progression of tumors, and may also be associated with neurodegenerative diseases and be involved in the pathogenesis of diseases such as Alzheimer's disease.
HSPA1A can protect cells from damage through synergistic effects with other molecular chaperones such as HSP70 and HSP40 under stressful conditions. In addition, it can also be involved in the regulation of apoptosis.
Yes, HSPA1A has therapeutic potential. In tumor therapy, drug suppression or gene therapy against HSPA1A may become a new way to treat tumors. At the same time, inhibitors against HSPA1A are also being developed.
Aberrant expression of HSPA1A may be associated with a variety of diseases, especially cancer, neurodegenerative diseases, etc. For example, in tumors such as lung, breast, and colon cancer, HSPA1A expression levels may be abnormally elevated.
Levels of HSPA1A can be detected by methods such as immunohistochemistry, western blotting, and real-time PCR, which can assess the amount of HSPA1A in tissues and cells.
This protein can bind to unfolded proteins to form multimeric complexes that facilitate proper folding and transport of proteins. In addition, it can also work synergistically with other molecular chaperones such as HSP70 and HSP40 to participate in the correct folding and transport of proteins.
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