Recombinant Human CRYAB Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1680NP
BL-1680NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1680NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human CRYAB Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1680NP
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Product Overview

Description Recombinant Human Crystalline Alpha -B Chain is produced by our E.coli expression system and the target gene encoding Met1-Lys175 is expressed with a 6His tag at the C-terminus.
Accession P02511
Synonym Alpha-Crystallin B Chain; Alpha(B)-Crystallin; Heat Shock Protein Beta-5; HspB5; Renal Carcinoma Antigen NY-REN-27; Rosenthal Fiber Component; CRYAB; CRYA2
Gene Background α Crystallin B Chain (CRYAB) is a cytoplasmic protein that belongs to the small heat shock protein (HSP20) family. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. Alpha crystallins acts as molecular chaperones and hold them in in large soluble aggregates. CRYAB is expressed widely in many tissues and organs. It may contribute to the transparency and refractive index of the lens. The deficiency of CRYAB is the cause of myopathy myofibrillar type 2 (MFM2) and cataract posterior polar type 2 (CTPP2).
Molecular Mass 21.22 KDa
Apmol Mass 25 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

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
Associated Diseases Myopathy, myofibrillar, 2 (MFM2); Cataract 16, multiple types (CTRCT16); Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB); Cardiomyopathy, dilated 1II (CMD1II)
Tissue Specificity Lens as well as other tissues. Expressed in myocardial tissue.

Gene Functions References

  1. alphaB-crystallin mutants carrying point substitutions in the C-terminal domain PMID: 28919577
  2. Heparan sulfate mediates cell uptake of alphaB-crystallin fused to the glycoprotein C cell penetration peptide PMID: 29408057
  3. Our findings suggest that serum level of miR-491 has potential as a biomarker for predicting OS progression and prognosis of OS patients. miR-491 exerts its role by directly targeting alphaB-crystallin (CRYAB) in OS. PMID: 28648665
  4. Study identified by a next-generation sequencing panel the novel CRYAB missense mutation c.326A>G, p.D109G in a small family with RCM in combination with skeletal myopathy with an early onset of the disease. PMID: 28493373
  5. Using a combination of co-sedimentation centrifugation, viscometric assays and electron microscopy of negatively stained filaments to analyse the in vitro assembly of desmin filaments, this study shows that the binding of CRYAB to desmin is subject to its assembly status, to the subunit organization within filaments formed and to the integrity of the C-terminal tail domain of desmin. PMID: 28470624
  6. Overexpression of both HSPB5 and Hsp27 significantly reduced the intracellular aggregation of alpha-synuclein. PMID: 28337642
  7. Glutathione-S-transferase - HspB1 fusion protein prevents more aggregation of malate dehydrogenase compared to glutathione-S-transferase -HspB5 fusion protein and wild type HspB1. PMID: 28130664
  8. Mechanistic studies revealed KLF4 specifically bound the promoter of CRYAB and upregulated CRYAB expression in human osteosarcoma cells. PMID: 27105535
  9. mRNA levels of HSP family members (HSP70B', HSP72, HSP40/DNAJ, and HSP20/CRYAB) are upregulated by the intracellular MMP3 overload. PMID: 27206651
  10. HspB5 maybe trigger the epithelial-mesenchymal transition in colorectal cancer (CRC) by activating the ERK signaling pathway. It is a potential tumor biomarker for CRC diagnosis and prognosis. PMID: 28796798
  11. The CLN6 is not only a molecular entity of the anti-aggregate activity conferred by the ER manipulation using TMalphaBC, but also serves as a potential target of therapeutic interventions. PMID: 28476624
  12. A missense mutation in alpha B-crystallin that changes proline 20 to an arginine leads to diminished anti-apoptotic activity compared with the native protein. PMID: 28007594
  13. phosphorylation finely regulates the chaperone activity of CRYAB with multipass TMPs and suggest a pivotal role for S59 in this process PMID: 27641668
  14. A missense mutation (p.D109G) in CRYAB causes restrictive cardiomyopathy (RCM). PMID: 28493373
  15. This work examines the molecular mechanism by which two canonical sHsps, alphaB-crystallin (alphaB-c) and Hsp27, interact with aggregation-prone alpha-syn to prevent its aggregation in vitro Both sHsps are very effective inhibitors of alpha-syn aggregation PMID: 27587396
  16. 343delT/343delT and WT KI/343delT-induced pluripotent stem cell-derived skeletal myotubes and cardiomyocytes did not express detectable levels of 343delT protein, contributable to the extreme insolubility of the mutant protein. Overexpression of HSPB5 343delT resulted in insoluble mutant protein aggregates and induction of a cellular stress response. PMID: 27226619
  17. Study suggests that wild-type and mutant alphaB-Cry have dissimilar secondary and tertiary structures. Moreover, alphaB-Cry indicates slightly improved chaperone activity upon the R12C mutation. These results may explain to some extent the non-cataractogenic nature of R12C mutation in aB-Cry. PMID: 27260392
  18. Cryab expression was elevated in osteosarcoma tissues and cell lines, and down-regulation of Cryab in MG-63 and U-2OS cells led to a decline in the cells' aggressiveness, and reduced secretion of matrix metalloproteinase-9 in vitro, and lower metastasis potential in vivo. PMID: 26789112
  19. Identifies alphaB-crystallin as a new binding partner for Nav1.5. alphaB-Crystallin interacts with Nav1.5 and increases INa by modulating the expression level and internalization of cell surface Nav1.5 and ubiquitination of Nav1.5, which requires the protein-protein interactions between alphaB-crystallin and Nav1.5 and between alphaB-crystallin and functionally active Nedd4-2. PMID: 26961874
  20. Alpha B-crystalline plays an important regulatory role in exosome biogenesis. PMID: 27129211
  21. alphaB-crystallin is an important regulator of epithelial-mesenchymal transition, acting as a molecular chaperone for SMAD4 and as its potential therapeutic target for preventing subretinal fibrosis development in neovascular age-related macular degeneration PMID: 26878210
  22. alpha B crystallin is an independent prognostic factor of infiltrating ductal carcinoma of the breast PMID: 26464626
  23. two novel missense mutations, p.R11C and p.R12C, in CRYAB associated with autosomal recessive congenital nuclear cataracts. PMID: 26402864
  24. Phosphorylation of alphaB-crystallin has dual role that manifests either beneficial or deleterious consequences depending on the extent of phosphorylation and interaction with cytoskeleton. [review] PMID: 26415747
  25. The multifunctional activity of human alphaB crystallin results from the interactive peptide sequences exposed on the surface of the molecule. [review] PMID: 26341790
  26. Data show that phosphorylation of crystallin alphaB (cryAB) deters its packaging into vesicles for exosomal secretion. PMID: 26620801
  27. CRYAB protein was up regulated in laryngeal squamous cell carcinoma. PMID: 24817638
  28. was It is markedly upregulated in the substantia nigra of PD patients where Cryab was present in glial cell inclusions. PMID: 25683516
  29. A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. PMID: 25962097
  30. These data suggest that alphaB-crystallin uses its inherent structural plasticity to expose distinct binding interfaces and thus interact with a wide range of structurally variable clients. PMID: 26458046
  31. findings point to alphaB-crystallin as a novel regulator of anoikis resistance that is induced by matrix detachment-mediated suppression of ERK signaling and promotes lung metastasis. PMID: 25684139
  32. Data suggest expression of CRYAB in endometrium in women with endometriosis may be biomarker for subsequent fertility; CRYAB levels in normal range (neither up- nor down-regulated) are indicative of fertility following medical or surgical treatment. PMID: 24945100
  33. we have summarized current data from emerging and exciting studies of the therapeutic strategies of alpha BC and alpha BC peptides and the efficient delivery strategies of these proteins in various disease models, including neurodegenerative diseases PMID: 25601468
  34. Study provides an accurate determination of the translational and rotational diffusion of alphaB-crystallin over a wide range of concentrations PMID: 25564856
  35. Results suggest a limited function of alphaB-crystallin and HSP27 in preventing abnormal tau protein deposition in glial cells and neurons; in addition, the expression of alphaB-crystallin phosphorylated at Ser59 may act as a protective factor in glial cells. PMID: 24985029
  36. results show that U373 cells produce and secrete CRYAB via exosomes and that stimulation with IL-1beta and TNF-alpha significantly increase the levels of CRYAB in not only the cells but also in the secreted exosomes PMID: 25261722
  37. CRYAB expression is correlated with substantial clinical characteristics of colorectal carcinoma, and it may be identified as an unfavorable prognostic factor for CRC. PMID: 25337251
  38. Raising the levels of CRYAB in spinal motor neurons by 6-fold did not delay paralysis in SOD1 transgenic mice. PMID: 25557022
  39. High expression of CRYAB was correlated with poor survival in non-small cell lung cancer patients. PMID: 25048725
  40. Mutations in CRYAB protein are a rare cause of genetically determined dilated cardiomyopathy. PMID: 23590293
  41. Data indicate that alpha-crystallin B chain and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp). PMID: 25450505
  42. Data suggest that inflammatory demyelination during multiple sclerosis is selectively associated with IFN-gamma-induced re-programming of an otherwise protective response of microglia and macrophages to the endogenous TLR2 agonist HSPB5 PMID: 24997049
  43. alphaB-crystallin hasa role in preventing protein aggregation by manipulation of the ER microenvironment PMID: 25449278
  44. This study reported a novel c.59C > G (P20R) missense mutation in CRYAB in a five-generation Chinese family with posterior polar cataract. PMID: 25195561
  45. strong prognostic marker for poor outcome in oral squamous cell carcinoma PMID: 24702231
  46. The higher expression of alphaB-crystallin may lead to prolonged survival of these cells under hypoxic conditions. PMID: 24725344
  47. investigated differences in protein expression levels in IDH1(R132H) mutant versus IDH1 wild type grade III gliomas; alphaB-crystallin proteins are elevated in IDH1(R132H) mutant tumors; expression appears to be controlled at post-translational level; most abundant form of alphaB-crystallin is a low molecular weight C-terminally truncated form PMID: 24473683
  48. Alpha B-crystallin has an essential role in TSC1/2 complex deficiency-mediated tumorigenesis. PMID: 24077282
  49. These findings provide novel insights into the role of p53 as a regulator of bidirectional gene pair HspB2/alpha B-crystallin-mediated ROS and the Warburg effect PMID: 24859470
  50. Crystallin alpha-B is increased in DNA microarray assays of papillary thyroid carcinoma PMID: 24880201


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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.

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