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ELK Biotechnology Crystallin-αB (phospho Ser59) rabbit pAb
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ELK Biotechnology Crystallin-αB (phospho Ser59) rabbit pAb

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Crystallin-αB (phospho Ser59) rabbit polyclonal antibody for IHC, IF, and ELISA applications. Recognizes phosphorylated Ser59 of human CRYAB. Useful for studying heat shock protein beta-5 localization and function. Stored at -20°C for long-term stability.

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pk
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ELK Biotechnology ES4832-100UL Crystallin-αB (phospho Ser59) rabbit pAb, 100UL pk판매 단위 pk ·
재고 확인 필요
402,000원VAT 포함 442,200원
ELK Biotechnology ES4832-50UL Crystallin-αB (phospho Ser59) rabbit pAb, 50UL pk판매 단위 pk ·
재고 확인 필요
301,000원VAT 포함 331,100원

ELK Biotechnology · ELK Biotechnology Crystallin-αB (phospho Ser59) rabbit pAb

제품명

Crystallin-αB (phospho Ser59) rabbit pAb

공급업체

ELK Biotechnology

제품 설명

Crystallin-αB (phospho Ser59)는 인간 CRYAB 단백질의 Ser59 인산화 부위를 인식하는 rabbit polyclonal antibody입니다. 이 항체는 heat shock protein beta-5로 알려진 CRYAB의 세포 내 위치 및 기능 연구에 적합합니다.

스펙 정보

항목 내용
Alternative Names CRYAB; CRYA2; Alpha-crystallin B chain; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component
Applications IHC; IF; ELISA
Recommended Dilutions Immunohistochemistry: 1/100 - 1/300
ELISA: 1/5000
Not yet tested in other applications
Immunogen Synthesized peptide derived from human CRYAB around phosphorylation site Ser59 (AA range: 31–80)
Host Rabbit
Storage -20°C / 1 year
Clonality Polyclonal
Isotype IgG
Concentration 1 mg/ml
GeneID (Human) 1410
Human Swiss-Prot No P02511
Species Reactivity Human; Mouse; Rat
Cellular Localization Cytoplasm, nucleus, secreted, lysosome. Translocates to the nucleus during heat shock and resides in SC35 speckles or nuclear splicing speckles. Localizes at Z-bands and intercalated disks in cardiomyocytes. Can be secreted via TMED10-dependent translocation through ERGIC and vesicle secretion.

배경 (Background)

Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins consist of two gene products: alpha-A and alpha-B, corresponding to acidic and basic forms. They are members of the small heat shock protein (HSP20) family and act as molecular chaperones by forming large soluble aggregates rather than renaturing proteins. These aggregates typically contain 30–40 subunits with an alpha-A to alpha-B ratio of 3:1. Alpha crystallins also possess autokinase activity and play roles in intracellular architecture. The encoded protein is considered a moonlighting protein due to its multifunctional nature.

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