Recombinant Bovine Alpha-Crystallin B Chain (CRYAB) Protein (His&Myc)

Name: Recombinant Bovine Alpha-Crystallin B Chain (CRYAB) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06924P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Bovine Alpha-Crystallin B Chain (CRYAB) 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	P02510
Target Symbol	CRYAB
Species	Bos taurus (Bovine)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPASTSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK
Expression Range	1-175aa
Protein Length	Full Length
Mol. Weight	27.5 kDa
Research Area	Cancer
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	May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
Subcellular Location	Cytoplasm. Nucleus. Secreted.
Protein Families	Small heat shock protein (HSP20) family
Database References	KEGG: bta:281719 STRING: 9913.ENSBTAP00000000556 UniGene: Bt.88059
Tissue Specificity	Lens as well as other tissues.

Gene Functions References

analysis of the structural, molecular and spectroscopic changes in alpha-crystallin protein as it slowly denatures due to aggregation induced by non-enzymatic glycation PMID: 26215735
The alphaB-crystallin content of bovine type I muscle fibers is quantitatively similar to that in the predominantly type I fibers of rat soleus muscle. PMID: 21975426
These results show that between pH 7 and 10 the protein undergoes a reversible thermal transition. PMID: 21445944
alpha-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration PMID: 21314599
In the presence of alpha-crystallin or GroEL the kinetic of GAPDH aggregation is changed from the diffusion-limited cluster-cluster aggregation to the reaction-limited cluster-cluster aggregation. PMID: 19936900
one of the functions of alphaB-crystallin is to bind microtubules via microtubule binding proteins and to give the MTs resistance to disassembly PMID: 15075233
The study provides evidence for the regulation of the chaperone activity of alphaB-crystallin by phosphorylation and indicates that this may play an important role in alleviating the pathogenic effects associated with protein conformational diseases. PMID: 16928191
analysis of alpha-crystallin assisted refolding of enzyme substrates PMID: 17211683
The results are consistent with the hypothesis that short-range, weak, attractive interactions between alpha- and gamma-crystallins are necessary for maximum transparency of the lens. PMID: 18509547

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.