Human Stress Induced Phosphoprotein 1 (STIP1) Protein
234€ (10 µg)
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name
Human Stress Induced Phosphoprotein 1 (STIP1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx168247
tested applications
WB, SDS-PAGE
Description
Stress Induced Phosphoprotein 1 Protein is a recombinant Human protein expressed in E. coli.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Stress Induced Phosphoprotein 1 (STIP1) |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 23.2 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Met1-Lys169 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 95% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Alias | STIP1,HEL-S-94n, HOP, IEF-SSP-3521, P60, STI1, STI1L, stress induced phosphoprotein 1 |
| Background | Protein STIP1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
STIP1 is a co-chaperone protein that coordinates the activities of heat shock proteins HSP70 and HSP90, facilitating protein folding, stability, and transport under stress conditions. It functions as a scaffold protein that regulates the transfer of client proteins between HSP70 and HSP90, ensuring proper protein maturation, stabilization, and degradation. STIP1 is ubiquitously expressed and is critical for processes such as protein quality control, cellular stress responses, and signal transduction. It also plays a role in cancer progression, where it stabilizes oncogenic signaling proteins and promotes tumor cell survival and proliferation. Dysregulation of STIP1 is associated with neurodegenerative diseases, such as Huntington's and Alzheimer's, where impaired chaperone function leads to protein aggregation and cellular dysfunction. Knockout studies reveal increased sensitivity to stress, defects in protein homeostasis, and impaired cell viability, emphasizing its role in protein folding, stress response, and maintaining cellular proteostasis.
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