ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
种属
Homo sapiens (Human)
性质
Recombinant
内毒素水平
Please contact with the lab for this information.
纯度
>90% as determined by SDS-PAGE.
预测分子量
44.68 kDa
状态
Lyophilized
保存溶液
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
重悬
Reconstitute in sterile water for a stock solution. Adjust the volume of sterile water so that, after reconstitution, the final stock concentration matches the value indicated on the product label or datasheet.
RECONSTITUTION PROTOCOL
1. Allow the product to be reconstituted and the reconstitution diluent to reach room temperature.
2. Tap or briefly centrifuge the product vial before opening to dislodge any lyophilized material that may be dispersed on the wall or cap of the vial.
3. Use the diluent and stock concentration recommended in the product datasheet. If preparing a stock concentration higher than recommended, contact Technical Service.
4. After adding the diluent, re-cap the vial and invert gently by hand or place on a slow rocking platform to allow the reconstitution diluent to coat all the surfaces inside the vial. Note: Do not mix by vortexing or by pipetting the material up and down.
5. Allow the vial to sit at room temperature with gentle agitation for at least 15 minutes before aliquotting or using.
6. Store the reconstituted material in single use aliquots in polypropylene or siliconized tubes. Aliquots of 10 μL or larger are recommended.
运输
In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
稳定性和存储
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
别名
HSP70B', HSPA6, Heat shock 70 kDa protein B', Heat shock 70 kDa protein 6
背景
Heat shock 70 kDa protein 6 (HSPA6) is a ~71 kDa protein. Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins.
