Recombinant Rhodopirellula baltica 60 kDa chaperonin 2 (groL2), partial

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Description

Rhodopirellula baltica

Rhodopirellula baltica is a marine bacterium known for its unique cellular structures and metabolic capabilities . It belongs to the Planctomycetes-Verrucomicrobia-Chlamydiae (PVC) superphylum and possesses a number of interesting features, including the ability to respond to environmental changes .

Chaperonins and GroL2

Chaperonins are a class of proteins that assist in the proper folding of other proteins, preventing aggregation and ensuring correct functionality . They are essential for cell survival, particularly under stress conditions. GroL2 is a specific type of chaperonin, a 60 kDa protein found in R. baltica .

Recombinant Production

Recombinant GroL2, partial, is produced through genetic engineering techniques, where the gene encoding a portion of the GroL2 protein is inserted into a host organism (e.g., Escherichia coli) or baculovirus system . The host organism then produces the protein, which is subsequently isolated and purified. The term "partial" indicates that the produced protein is not the full-length GroL2 but a fragment of it.

Function and Significance

Chaperonins like GroL2 are crucial for protein homeostasis within the cell. They are often upregulated under stress conditions, such as nutrient limitation, to maintain the correct folding of proteins and prevent aggregation .

R. baltica cells adapt metabolically to nutrient limitation by inducing chaperones .

Applications and Research

Studying recombinant GroL2, partial, can provide insights into:

  • The structure and function of chaperonins.

  • The stress response mechanisms in R. baltica .

  • Potential biotechnological applications, such as protein folding and drug discovery.

Data Table: Gene Expression Studies in R. baltica

Number of regulated genes62 h vs. 44 h82 h vs. 62 h96 h vs. 82 h240 h vs. 82 h
Total (%) *149 (2%)90 (1%)235 (3%)863 (12%)
Encoding hypothetical proteins (%) **84 (56%)40 (44%)139 (59%)499 (58%)

* (%) relative to the total number of 7325 open reading frames (ORFs) annotated in R. baltica genome.

** (%) relative to the total number of regulated genes.

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your format preference during order placement for customized preparation.
Lead Time
Delivery times vary depending on the purchasing method and location. Please consult your local distributor for precise delivery estimates.
Note: All proteins are shipped with standard blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to consolidate the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our standard glycerol concentration is 50% and serves as a guideline.
Shelf Life
Shelf life depends on several factors including storage conditions, buffer components, temperature, and the protein's inherent stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized forms have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquoting is essential for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing.
The tag type is determined during production. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
groL2; groEL2; RB897060 kDa chaperonin 2; GroEL protein 2; Protein Cpn60 2
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Protein Length
Partial
Purity
>85% (SDS-PAGE)
Species
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Target Names
groL2
Uniprot No.

Target Background

Function
In conjunction with its co-chaperonin GroES, this protein plays a crucial role in protein folding. The GroEL-GroES system forms a nano-cage that encapsulates unfolded proteins, providing an optimized environment to promote and accelerate their folding.
Database Links

KEGG: rba:RB8970

STRING: 243090.RB8970

Protein Families
Chaperonin (HSP60) family
Subcellular Location
Cytoplasm.

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