Recombinant Human Alpha-Crystallin B Chain (CRYAB)

Name: Recombinant Human Alpha-Crystallin B Chain (CRYAB)
Brand: Beta LifeScience
SKU: BLC-11276P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Alpha-Crystallin B Chain (CRYAB) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P02511
Target Symbol	CRYAB
Synonyms	AACRYA; Alpha B crystallin; Alpha crystallin B chain; Alpha(B)-crystallin; Alpha-crystallin B chain; CRYA2; Cryab; CRYAB_HUMAN; Crystallin alpha B; Crystallin alpha polypeptide 2; CTPP2; Heat shock 20 kD like protein; Heat shock protein beta 5; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY REN 27; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Expression Range	1-175aa
Protein Length	Full Length
Mol. Weight	20.2 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.
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	HGNC: 2389 OMIM: 123590 KEGG: hsa:1410 STRING: 9606.ENSP00000227251 UniGene: PMID: 28919577 Heparan sulfate mediates cell uptake of alphaB-crystallin fused to the glycoprotein C cell penetration peptide PMID: 29408057 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 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 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 Overexpression of both HSPB5 and Hsp27 significantly reduced the intracellular aggregation of alpha-synuclein. PMID: 28337642 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 Mechanistic studies revealed KLF4 specifically bound the promoter of CRYAB and upregulated CRYAB expression in human osteosarcoma cells. PMID: 27105535 mRNA levels of HSP family members (HSP70B', HSP72, HSP40/DNAJ, and HSP20/CRYAB) are upregulated by the intracellular MMP3 overload. PMID: 27206651 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 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 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 phosphorylation finely regulates the chaperone activity of CRYAB with multipass TMPs and suggest a pivotal role for S59 in this process PMID: 27641668 A missense mutation (p.D109G) in CRYAB causes restrictive cardiomyopathy (RCM). PMID: 28493373 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 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 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 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 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 Alpha B-crystalline plays an important regulatory role in exosome biogenesis. PMID: 27129211 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 alpha B crystallin is an independent prognostic factor of infiltrating ductal carcinoma of the breast PMID: 26464626 two novel missense mutations, p.R11C and p.R12C, in CRYAB associated with autosomal recessive congenital nuclear cataracts. PMID: 26402864 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 The multifunctional activity of human alphaB crystallin results from the interactive peptide sequences exposed on the surface of the molecule. [review] PMID: 26341790 Data show that phosphorylation of crystallin alphaB (cryAB) deters its packaging into vesicles for exosomal secretion. PMID: 26620801 CRYAB protein was up regulated in laryngeal squamous cell carcinoma. PMID: 24817638 was It is markedly upregulated in the substantia nigra of PD patients where Cryab was present in glial cell inclusions. PMID: 25683516 A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. PMID: 25962097 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 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 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 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 Study provides an accurate determination of the translational and rotational diffusion of alphaB-crystallin over a wide range of concentrations PMID: 25564856 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 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 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 Raising the levels of CRYAB in spinal motor neurons by 6-fold did not delay paralysis in SOD1 transgenic mice. PMID: 25557022 High expression of CRYAB was correlated with poor survival in non-small cell lung cancer patients. PMID: 25048725 Mutations in CRYAB protein are a rare cause of genetically determined dilated cardiomyopathy. PMID: 23590293 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 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 alphaB-crystallin hasa role in preventing protein aggregation by manipulation of the ER microenvironment PMID: 25449278 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 strong prognostic marker for poor outcome in oral squamous cell carcinoma PMID: 24702231 The higher expression of alphaB-crystallin may lead to prolonged survival of these cells under hypoxic conditions. PMID: 24725344 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 Alpha B-crystallin has an essential role in TSC1/2 complex deficiency-mediated tumorigenesis. PMID: 24077282 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 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.