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BRAND / VENDOR: Abcam

Abcam, ab316552, Recombinant Human DR4 Protein Standard

CATALOG NUMBER: ab316552
السعر العادي$0.99
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Product Description

Size: 10µg
Recombinant Human DR4 Protein Standard is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.
Key facts
Purity:>80% SDS-PAGE,
Expression system:HEK 293 cells,
Tags:Tag free,
Applications:sELISA, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:O00220,
Animal free:Yes,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.3 - 7.5Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

Product details:
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
DR4 also known as TRAIL-R1 is a receptor with a molecular weight of approximately 60 kDa. It is part of the tumor necrosis factor receptor (TNFR) superfamily. DR4 is widely expressed in various types of tissues such as the liver spleen thymus and peripheral blood leukocytes. It functions mechanically by binding to its ligand TNF-related apoptosis-inducing ligand (TRAIL) which initiates signaling cascades that lead to apoptosis or programmed cell death.
Biological function summary
The death receptor 4 plays an important role in mediating cell apoptosis. Upon ligand binding DR4 interacts with the adapter molecule FADD (FAS-associated protein with death domain) facilitating the formation of the death-inducing signaling complex (DISC). This complex recruits and activates caspase-8 which eventually leads to the activation of the downstream effector caspases driving the cell towards apoptosis. DR4 operates as a significant component of the extrinsic pathway of apoptosis a process important for maintaining cellular homeostasis and eliminating harmful cells.
Pathways
DR4 functions critically within the extrinsic apoptotic pathway. This pathway involves other death receptors such as DR5 which also binds TRAIL similarly leading to apoptosis through DISC formation and caspase activation. The extrinsic pathway interconnects with the intrinsic pathway via the mitochondria with proteins like Bid acting as a bridge between them. The engagement of these pathways highlights DR4’s importance in regulatory mechanisms of cell death tightly controlling cellular proliferation and survival.
DR4 plays a significant role in cancer and autoimmune diseases. Alterations in DR4 expression or function can lead to evasion of apoptosis by cancer cells contributing to tumor progression. The defective apoptotic signaling via DR4 is also linked to autoimmune disorders where insufficient apoptosis may allow for the survival of autoreactive immune cells. In both scenarios DR4's involvement usually associates with its counterpart DR5 as they share similar ligand-binding properties and signal transduction mechanisms in diseased states.


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Collaboration

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