人 Calreticulin 抗体对
01AB04178
Calreticulin (CALR) is a multifunctional protein primarily localized in the endoplasmic reticulum (ER), where it serves as a calcium-binding chaperone essential for protein folding and quality control. CALR consists of three distinct domains: an N-terminal domain that facilitates ER localization, a middle proline-rich domain that exhibits lectin-like chaperone activity, and a C-terminal domain containing multiple calcium-binding sites. This protein plays a critical role in maintaining calcium homeostasis within the ER. Beyond its chaperone functions, CALR is also involved in modulating immune responses and cellular metabolism. Its ability to interact with misfolded proteins prevents their export from the ER, thereby ensuring proper protein synthesis and function. Dysregulation of CALR has been linked to several diseases, particularly myeloproliferative neoplasms (MPNs), where somatic mutations in the CALR gene contribute to disease pathogenesis. CALR's role in regulating immune responses has implications in cancer, as it can influence tumor progression and immune evasion.
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技术参数
- 靶点基因名
- CALR
- 基因别名
- CRTC
- 蛋白别名
- calreticulin; Calreticulin
- UniProt
- P27797
- 物种
- Human
产品详情
- 靶点名称
- Calreticulin
- 蛋白名称
- calreticulin
- 蛋白别名
- Calreticulin; CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP; grp60
- 靶点基因名
- CALR
- 基因别名
- CRTC
- UniProt
- P27797
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Calreticulin (CALR) is a multifunctional protein primarily localized in the endoplasmic reticulum (ER), where it serves as a calcium-binding chaperone essential for protein folding and quality control. CALR consists of three distinct domains: an N-terminal domain that facilitates ER localization, a middle proline-rich domain that exhibits lectin-like chaperone activity, and a C-terminal domain containing multiple calcium-binding sites. This protein plays a critical role in maintaining calcium homeostasis within the ER. Beyond its chaperone functions, CALR is also involved in modulating immune responses and cellular metabolism. Its ability to interact with misfolded proteins prevents their export from the ER, thereby ensuring proper protein synthesis and function. Dysregulation of CALR has been linked to several diseases, particularly myeloproliferative neoplasms (MPNs), where somatic mutations in the CALR gene contribute to disease pathogenesis. CALR's role in regulating immune responses has implications in cancer, as it can influence tumor progression and immune evasion.