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AB238223

Recombinant clpP2 protein (Tagged)

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Recombinant clpP2 protein (Tagged) is a Borreliella burgdorferi B31 Full Length protein, in the 1 to 198 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

clpP-2, BB_0757, clpP2, ATP-dependent Clp protease proteolytic subunit 2, Endopeptidase Clp 2

1 Images
SDS-PAGE - Recombinant clpP2 protein (Tagged) (AB238223)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant clpP2 protein (Tagged) (AB238223)

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab238223.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

10x His tag N-Terminus Myc tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

O51698

Animal free

No

Carrier free

No

Species

Borreliella burgdorferi B31

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

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>" } } }

Sequence info

[{"sequence":"MTGKEDNDACVLHDKSLKLVLKSRSIVIAGEITKDVSRLFQEKILLLEALDFKKPIFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTVGVGLVASAAALIFLAAKLENRFSLPFARYLLHQPLSGFKGVATDIEIYTNELNKVKKELNNIISKETGQKISKIEKDTDRDFWLDSSAAKKYGLVFEVVETKYQLEEFISA","proteinLength":"Full Length","predictedMolecularWeight":"27.2 kDa","actualMolecularWeight":null,"aminoAcidEnd":198,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O51698","tags":[{"tag":"10x His","terminus":"N-Terminus"},{"tag":"Myc","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

ClpP2 also called Caseinolytic Peptidase P2 is a mitochondrial enzyme with an approximate molecular mass of 28.5 kDa. This protein participates in the degradation of misfolded and damaged proteins within the chloroplast and is expressed across various plant species. ClpP2 constitutes part of the multisubunit protease complex facilitating proteolytic cleavage through its catalytic activity. This protease function is essential for maintaining protein homeostasis within the chloroplast.
Biological function summary

ClpP2 acts as an integral component of the Clp proteolytic complex responsible for protein quality control. This complex with multiple Clp proteins degrades unwanted proteins for cellular regulation and proper function. As part of the Clp complex ClpP2 ensures selective degradation sustaining cellular health. Through these processes it supports various cellular functions including photosynthesis and stress responses by modulating protein concentration and removing damaged polypeptides.

Pathways

ClpP2 involves itself in the chloroplast proteostasis pathway. This pathway is particularly key in maintaining functionality under stress conditions impacting photosynthesis and plant growth. ClpP2 interacts with proteins such as FtsH and Lon proteases which play roles in the same proteolytic systems. This links ClpP2 to important pathways controlling chloroplast and plant vitality.

ClpP2's dysfunction can lead to impaired chloroplast development and function in plants affecting photosynthesis and growth. Aberrations in ClpP2 expression or mutations may relate to chlorosis where plants display a deficiency in chlorophyll leading to pale-colored leaves. The ClpP2 protein through its association with ClpC and ClpD proteins has connections to these developmental issues highlighting the importance of protein degradation in plant health.

Specifications

Form

Liquid

General info

Function

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.

Sequence similarities

Belongs to the peptidase S14 family.

Product protocols

Target data

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
See full target information clpP2

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