Recombinant Rat Heat Shock Protein Beta-6 (HSPB6) Protein (His)

Name: Recombinant Rat Heat Shock Protein Beta-6 (HSPB6) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00275P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Heat Shock Protein Beta-6 (HSPB6) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P97541
Target Symbol	HSPB6
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	MEIRVPVQPSWLRRASAPLPGFSTPGRLFDQRFGEGLLEAELASLCPAAIAPYYLRAPSVALPTAQVPTDPGYFSVLLDVKHFSPEEISVKVVGDHVEVHARHEERPDEHGFIAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQATPASAQASLPSPPAAK
Expression Range	1-162aa
Protein Length	Full Length
Mol. Weight	24.4 kDa
Research Area	Others
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	Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.
Subcellular Location	Cytoplasm. Nucleus. Secreted.
Protein Families	Small heat shock protein (HSP20) family
Database References	KEGG: rno:192245 STRING: 10116.ENSRNOP00000028401 UniGene: Rn.3201
Tissue Specificity	Widely expressed. High expression in muscle tissues.

Gene Functions References

we show for the first time that alphaB-crystallin, a molecular chaperon for tubulin/microtubules, is involved in cell shape determination. knockdown of this molecule caused myoblasts and glioma cells to lose their ability for adhesion as they tended to behave like migratory cells. knockdown in both C6 glial cells and L6 myoblast permitted cells to migrate more rapidly than dermal fibroblasts. PMID: 27977738
formation of the Hsp20-PKD1 complex is essential for PKD1 nuclear translocation, signaling mechanisms leading to hypertrophy PMID: 25889640
Localization, macromolecular associations, and function of HSP20 in the heart. PMID: 12551873
After 7 days of spinal cord transection, Hsp20 and Hsp25 levels in the soleus, plantaris, and adductor longus muscles were lower than in control rats, whereas Hsp20 was unchanged and Hsp25 increased in the tibialis anterior. PMID: 15221884
Secreased HSP20 is mediated by cAMP-dependent pathway, and impaired vasoconstriction in portal hypertension may be partially explained by decreased HSP20. Phosphorylation of HSP20 by PKA may alter HSP20 turnover. PMID: 15513950
Overexpression of Hsp20 inhibits doxorubicin-triggered cardiac injury, an effect that is dependent on AKT activation. PMID: 18948619
Here, crystal structures of excised alpha-crystallin domain from rat Hsp20 and that from human alphaB-crystallin show that they form homodimers with a shared groove at the interface by extending a beta sheet. PMID: 19646995

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.