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Mouse Anti-CRYAB Recombinant Antibody (3 E3) (CBMAB-C5433-LY)

This product is antibody recognizes CRYAB. The antibody 3 E3 immunoassay techniques such as: WB.
See all CRYAB antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3 E3
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
CRYAB antibody was raised in mouse using a protein expressed in 293T cell transfected with human CRYAB expression vector as the immunogen
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
0.5 mg/mL-1 mg/ml
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Crystallin Alpha B
Introduction
CRYAB (Crystallin Alpha B) is a Protein Coding gene. Diseases associated with CRYAB include Myopathy, Myofibrillar, 2 and Cataract 16, Multiple Types. Among its related pathways are Protein processing in endoplasmic reticulum and Longevity regulating pathway. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and microtubule binding.
An important paralog of this gene is CRYAA.
Entrez Gene ID
1410
UniProt ID
P02511
Alternative Names
Crystallin Alpha B; Renal Carcinoma Antigen NY-REN-27; Heat Shock Protein Beta-5; Rosenthal Fiber Component; CRYA2; HSPB5; Epididymis Secretory Protein Li 101; Heat-Shock 20 KD Like-Protein; Alpha-Crystallin B Chain;
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.
Biological Process
Apoptotic process involved in morphogenesis Source: Ensembl
Cellular response to gamma radiation Source: MGI
Lens development in camera-type eye Source: Ensembl
Microtubule polymerization or depolymerization Source: Ensembl
Multicellular organism aging Source: Ensembl
Muscle contraction Source: ProtInc
Muscle organ development Source: Ensembl
Negative regulation of amyloid fibril formation Source: ARUK-UCL
Negative regulation of apoptotic process Source: HGNC-UCL
Negative regulation of cell growth Source: Ensembl
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
Negative regulation of gene expression Source: Ensembl
Negative regulation of intracellular transport Source: HGNC-UCL
Negative regulation of protein-containing complex assembly Source: ARUK-UCL
Negative regulation of reactive oxygen species metabolic process Source: Ensembl
Negative regulation of transcription, DNA-templated Source: UniProtKB
Protein folding Source: ProtInc
Protein stabilization Source: CAFA
Regulation of cell death Source: MGI
Regulation of cellular response to heat Source: Reactome
Response to estradiol Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to hypoxia Source: Ensembl
Stress-activated MAPK cascade Source: Ensembl
Tubulin complex assembly Source: Ensembl
Cellular Location
Cytoplasm; Nucleus; Secreted. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (PubMed:19464326). Localizes at the Z-bands and the intercalated disk in cardiomyocytes (PubMed:28493373). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059).
Involvement in disease
Myopathy, myofibrillar, 2 (MFM2):
A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM2 is characterized by weakness of the proximal and distal limb muscles, weakness of the neck, velopharynx and trunk muscles, hypertrophic cardiomyopathy, and cataract in a subset of patients.
Cataract 16, multiple types (CTRCT16):
An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT16 includes posterior polar cataract, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens.
CRYAB mutations may be involved in restrictive cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM is characterized by restrictive ventricular-filling physiology in the presence of normal or reduced diastolic and/or systolic volumes (of 1 or both ventricles), biatrial enlargement, and normal ventricular wall thickness.
Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB):
A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFMFIH-CRYAB has onset in the first weeks of life after a normal neonatal period. Affected infants show rapidly progressive muscular rigidity of the trunk and limbs associated with increasing respiratory difficulty resulting in death before age 3 years.
Cardiomyopathy, dilated 1II (CMD1II):
A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.

Pagano, C., Navarra, G., Gazzerro, P., Vitale, M., Notarnicola, M., Caruso, M. G., ... & Bifulco, M. (2021). Association of alpha B-crystallin expression with tumor differentiation grade in colorectal cancer patients. Diagnostics, 11(5), 896.

Yang, M., Li, Y., & Tian, F. (2021). Association between Alpha B-crystallin expression and prognosis in patients with solid tumors: A protocol for systematic review and meta-analysis. Medicine, 100(7).

Bao, Q., Yang, D., Hong, F., Yang, J., Li, L., Jin, Y., & Ma, C. (2019). αB-crystallin (CRYAB) regulates the proliferation, apoptosis, synthesis and degradation of extracellular matrix of chondrocytes in osteoarthritis. Experimental Cell Research, 382(2), 111459.

Lu, S. Z., Guo, Y. S., Liang, P. Z., Zhang, S. Z., Yin, S., Yin, Y. Q., ... & Zhou, J. W. (2019). Suppression of astrocytic autophagy by αB-crystallin contributes to α-synuclein inclusion formation. Translational Neurodegeneration, 8(1), 1-14.

Guo, Y. S., Liang, P. Z., Lu, S. Z., Chen, R., Yin, Y. Q., & Zhou, J. W. (2019). Extracellular αB-crystallin modulates the inflammatory responses. Biochemical and biophysical research communications, 508(1), 282-288.

Tan, L., Sha, L., Hou, N., Zhang, M., Ma, Q., & Shi, C. (2019). High α B-crystallin and p53 co-expression is associated with poor prognosis in ovarian cancer. Bioscience reports, 39(6).

D’Agostino, M., Scerra, G., Cannata Serio, M., Caporaso, M. G., Bonatti, S., & Renna, M. (2019). Unconventional secretion of α-Crystallin B requires the Autophagic pathway and is controlled by phosphorylation of its serine 59 residue. Scientific reports, 9(1), 1-14.

Chen, D., Cao, G., Qiao, C., Liu, G., Zhou, H., & Liu, Q. (2018). Alpha B‐crystallin promotes the invasion and metastasis of gastric cancer via NF‐κB‐induced epithelial‐mesenchymal transition. Journal of Cellular and Molecular Medicine, 22(6), 3215-3222.

Shi, C., Yang, X., Bu, X., Hou, N., & Chen, P. (2017). Alpha B-crystallin promotes the invasion and metastasis of colorectal cancer via epithelial-mesenchymal transition. Biochemical and biophysical research communications, 489(4), 369-374.

Fichna, J. P., Potulska-Chromik, A., Miszta, P., Redowicz, M. J., Kaminska, A. M., Zekanowski, C., & Filipek, S. (2017). A novel dominant D109A CRYAB mutation in a family with myofibrillar myopathy affects αB-crystallin structure. BBA clinical, 7, 1-7.

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For research use only. Not intended for any clinical use.

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