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AB202201

Recombinant Human CASP protein (denatured) (His tag N-Terminus)

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Recombinant Human CASP protein (denatured) (His tag N-Terminus) is a Human Full Length protein, in the 1 to 359 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

PSCDBP, CYTIP, Cytohesin-interacting protein, Cytohesin binder and regulator, Cytohesin-associated scaffolding protein, Cytohesin-binding protein HE, Pleckstrin homology Sec7 and coiled-coil domains-binding protein, CYBR, CASP, Cbp HE

1 Images
SDS-PAGE - Recombinant Human CASP protein (denatured) (His tag N-Terminus) (AB202201)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human CASP protein (denatured) (His tag N-Terminus) (AB202201)

15% SDS-PAGE analysis of ab202201 (3 μg).

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

O60759

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Protein previously labeled as PSCDBP.

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPPGSHMGSEFMSLQRLLQHSSNGNLADFCAGPAYSSYSTLTGSLTMDDNRRIQMLADTVATLPRGRKQLALTRSSSLSDFSWSQRKLVTVEKQDNETFGFEIQSYRPQNQNACSSEMFTLICKIQEDSPAHCAGLQAGDVLANINGVSTEGFTYKQVVDLIRSSGNLLTIETLNGTMILKRTELEAKLQVLKQTLKQKWVEYRSLQLQEHRLLHGDAANCPSLENMDLDELSLFGPLPGPGPALVDRNRLSSESSCKSWLSSMTMDSEDGYQTCVSEDSSRGAFSRQTSTDDECFIPKEGDDFLRRSSSRRNRSISNTSSGSMSPLWEGNLSSMFGTLPRKSRKGSVRKQLLKFIPGLHRAVEEEESRF","proteinLength":"Full Length","predictedMolecularWeight":"42.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":359,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O60759","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

CASP also known as caspase is a family of cysteine-aspartic proteases. These proteins typically have a mass between 20 and 30 kDa. CASP proteins primarily occur in the cytoplasm of cells. They perform important roles in apoptosis or programmed cell death by cleaving specific substrates in the cell leading to the orderly disassembly of cellular components. CASP enzymes become activated by proteolytic processing when a cell receives apoptotic signals leading to their role as executioners in the apoptosis process.
Biological function summary

CASP proteins serve as key mediators in apoptosis and inflammation. They are members of the caspase cascade an essential cell signaling pathway. These proteins can be activated in response to specific cellular stress signals often forming complexes like the apoptosome with other molecules such as cytochrome c and APAF1. The formation of these complexes allows CASP proteins to regulate the cell fate and maintain cellular homeostasis limiting excessive inflammation and tissue damage.

Pathways

CASP proteins play roles in both the intrinsic and extrinsic apoptotic pathways. In the extrinsic pathway signals are received through death receptors leading to the activation of initiator caspases like CASP8. Subsequent cleavage and activation of effector caspases such as CASP3 and CASP7 occur. In the intrinsic pathway CASP9 becomes activated through mitochondrial signals and then facilitates activation of downstream effector caspases. These pathways ensure that CASP proteins interconnect with various pro-apoptotic and anti-apoptotic proteins to effectuate cell death.

Dysregulation of CASP proteins links to conditions such as cancer and neurodegenerative diseases. For instance reduced caspase activity can allow survival of damaged cells contributing to cancer development and progression. Conversely excessive caspase activation is implicated in diseases like Alzheimer's where neuronal cell death results in cognitive decline. BCL2 proteins interact importantly with CASP pathways and influence apoptotic responses highlighting the involvement of this network in disease pathogenesis.

Specifications

Form

Liquid

General info

Function

By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm.

Subcellular localisation

Early endosome

Product protocols

Target data

By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm.
See full target information CYTIP

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