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Recombinant Escherichia coli Chaperone-like protein hdeA (hdeA)

Recombinant Escherichia coli Chaperone-like protein hdeA (hdeA)

Code	CSB-YP360159ENV
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP360159ENV
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP360159ENV-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP360159ENV
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP360159ENV
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

hdeA

Uniprot No.

P0AES9

Alternative Names

hdeA; yhhC; yhiB; b3510; JW3478; Acid stress chaperone HdeA; 10K-S protein

Species

Escherichia coli (strain K12)

Expression Region

22-110

Target Protein Sequence

ADAQKAADN KKPVNSWTCE DFLAVDESFQ PTAVGFAEAL NNKDKPEDAV LDVQGIATVT PAIVQACTQD KQANFKDKVK GEWDKIKKDM

Protein Length

Full Length of Mature Protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Required for optimal acid stress protection. Exhibits a chaperone-like activity only at pH below 3 by suppressing non-specifically the aggregation of denaturated periplasmic proteins. Important for survival of enteric bacteria in the acidic environment of the host stomach. Also promotes the solubilization at neutral pH of proteins that had aggregated in their presence at acidic pHs. May cooperate with other periplasmic chaperones such as DegP and SurA.

Gene References into Functions

HdeA binds its substrates heterogeneously, and the "amphiphilic" model for HdeA-substrate interaction is discussed. PMID: 29016106
HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA. PMID: 26593705
these results provide insight into the process by which HdeA is primed to unfold and carry out its chaperone duties below pH 3.0 PMID: 24375557
The small periplasmic chaperone HdeA is directly activated by partial unfolding in a low ph environment. PMID: 23487787
The authors conclude that E. coli O157:H7 strains have evolved acid survival strategies independent of the HdeA/B chaperones and are more acid resistant than nonpathogenic K-12. PMID: 22179243
HdeA exposes hydrophobic surfaces that appear to be involved in the binding of denatured substrate proteins at extremely low pH values PMID: 15911614
HdeA and HdeB not only help to maintain proteins in a soluble state during acid treatment, as previously reported, but also assist, both in vitro and in vivo, in the solubilization at neutral pH of mixed protein-chaperone aggregates formed at acidic pH PMID: 18359765
the partially unfolded character of active HdeA allows the chaperone to adopt different conformations as required for the recognition and high-affinity binding of different substrate proteins. PMID: 19321422