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          • Proteins & Peptides ›
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          CRYAB Proteins

          CRYAB Human recombinant proteins are validated for use in the following applications: Neutralization. Available Product Grades: Research Use Only. Browse 1 protein. Not finding the exact protein, grade or size needed?... CRYAB Human recombinant proteins are validated for use in the following applications: Neutralization. Available Product Grades: Research Use Only. Browse 1 protein. Not finding the exact protein, grade or size needed? Contact us... CRYAB Human recombinant proteins are validated for use in the following applications: Neutralization. Available Product Grades: Research Use Only. Browse 1 protein. Not finding the exact protein, grade or size needed? Contact us to discuss your specific application and product needs.... CRYAB Human recombinant proteins are validated for use in the following applications: Neutralization. Available Product Grades: Research Use Only. Browse 1 protein. Not finding the exact protein, grade or size needed? Contact us to discuss your specific application and product needs.

          Protein Information

          Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products-alpha-A and alpha-B. There are at least 5 different proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identified in bovine and rat lens. Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander's disease where it accumulates in brain cells of those afflicted.

          Synonyms

          2310001E10Rik; 3526402H21Rik; AACRYA; active transcription factor CREB; alpha B-crystallin; alpha crystallin B; alpha(B)-crystallin; alpha-B-crystallin; Alpha-crystallin B chain; alpha-crystallin B chain-like protein; AV083133; cAMP response element binding protein 1; cAMP responsive element binding protein 1; cAMP-response element-binding protein-1; cAMP-responsive element-binding protein 1; CMD1II; CREB; CREB1; CREB-1; Crya2; Crya-2; CRYAB; CryAB antibody; crystallin alpha B; crystallin, alpha 2; crystallin, alpha B; crystallin, alpha polypeptide 2; CTPP2; CTRCT16; cyclic adenosine 3',5'-monophosphate response element-binding protein CREB; cyclic AMP-responsive element-binding protein 1; epididymis secretory protein Li 101; heat shock protein beta-5; heat shock protein CryAB; heat shock protein HspB5; heat-shock 20 kD like-protein; HEL-S-101; HSPB5; HspB5 protein; MFM2; P23; Renal carcinoma antigen NY-REN-27; rosenthal fiber component; transactivator protein; Y protein

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          Clicking the images or links will redirect you to a website hosted by BenchSci that provides third-party scientific content. Neither the content nor the BenchSci technology and processes for selection have been evaluated by us; we are providing them as-is and without warranty of any kind, including for use or application of the Thermo Fisher Scientific products presented.

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          Invitrogen
          Human CRYAB (aa 121-172) Control Fragment Recombinant Protein
          Invitrogen
          Human CRYAB (aa 121-172) Control Fragment Recombinant Protein
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          Human
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          Cat # RP-104094

          100 µL

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