Stress Induced Phosphoprotein 1 (STIP1) Antibody

819€ (1 ml)
Por favor contáctenos para obtener información detallada sobre el precio y disponibilidad.
935106861
info@markelab.com
name
Stress Induced Phosphoprotein 1 (STIP1) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx174651
tested applications
WB, IHC, IF/ICC
Description
This product is currently in development. The lead time for this product may be several months. Please contact us at
Documents del producto
Instrucciones
Data sheet
Product specifications
Category | Primary Antibodies |
Immunogen Target | Stress Induced Phosphoprotein 1 (STIP1) |
Host | Mouse |
Reactivity | Human |
Recommended Dilution | WB: 0.01-2 µg/ml, IHC: 5-20 µg/ml, IF/ICC: 5-20 µg/ml. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Monoclonal |
Conjugation | Unconjugated |
Purification | Purified by Protein A and Protein G affinity chromatography. |
Size 1 | 1 ml |
Form | Liquid |
Tested Applications | WB, IHC, IF/ICC |
Buffer | 0.01 M PBS, pH 7.4, containing 0.05% Proclin-300, 50% glycerol. |
Availability | Please enquire. |
Storage | Aliquot and store at -20°C. 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 | Antibody anti-STIP1 |
Status | RUO |
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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