Recombinant Arabidopsis Thaliana Heat Shock Protein 21, Chloroplastic (HSP21) Protein (His&Myc)

Name: Recombinant Arabidopsis Thaliana Heat Shock Protein 21, Chloroplastic (HSP21) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01775P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Arabidopsis Thaliana Heat Shock Protein 21, Chloroplastic (HSP21) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P31170
Target Symbol	HSP21
Synonyms	25.3 kDa heat shock protein, chloroplastic
Species	Arabidopsis thaliana (Mouse-ear cress)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AQDQRENSIDVVQQGQQKGNQGSSVEKRPQQRLTMDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDTMPVSGRNRGGSGVSEIRAPWDIKEEEHEIKMRFDMPGLSKEDVKISVEDNVLVIKGEQKKEDSDDSWSGRSVSSYGTRLQLPDNCEKDKIKAELKNGVLFITIPKTKVERKVIDVQIQ
Expression Range	44-227aa
Protein Length	Full Length of Mature Protein
Mol. Weight	28.4 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Chaperone protein required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription.
Subcellular Location	Plastid, chloroplast stroma, chloroplast nucleoid.
Protein Families	Small heat shock protein (HSP20) family
Database References	KEGG: ath:AT4G27670 STRING: 3702.AT4G27670.1 UniGene: At.5368
Tissue Specificity	Confined to pollen grains of budding flowers.

Gene Functions References

plastid-localized metalloprotease FtsH6 regulates HSP21 abundance. Lack of a functional FtsH6 protein promotes HSP21 accumulation during the later stages of thermomemory and increases thermomemory capacity. PMID: 27561243
Findings reveal an auto-adaptation loop pathway that plant cells optimize particular needs of chloroplasts in stabilizing photosynthetic complexes by relaying the GUN5-dependent plastid signal(s) to activate the heat-responsive expression of HSP21 in the nucleus during adaptation to heat stress in plants. PMID: 27943531
Studied Hsp21 association with thylakoid membranes in heat stress resistance of Arabidopsis thaliana. PMID: 28608391
analysis of the structure of dodecameric heat-shock protein Hsp21 PMID: 28325834
Present a structure model of Arabidopsis thaliana Hsp21, obtained by homology modeling, single-particle electron microscopy, and lysine-specific chemical crosslinking. PMID: 21280121
evolution of a pseudogene: diversity and divergence of HSP21 PMID: 18356953

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.