产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
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Heat shock 27kDa protein; 28 kDa heat shock protein; CMT2F; DKFZp586P1322; epididymis secretory protein Li 102; Estrogen regulated 24 kDa protein; Estrogen-regulated 24 kDa protein; Heat shock 25kDa protein 1; Heat shock 27 kDa protein; Heat shock 27kD protein 1; Heat shock 27kDa protein 1; Heat shock 28kDa protein 1; Heat Shock Protein 27; Heat shock protein beta 1; Heat shock protein beta-1; heat shock protein family B (small) member 1; HEL-S-102; HMN2B; HS.76067; Hsp 25; HSP 27; Hsp 28; Hsp B1; Hsp25; HSP27; Hsp28; HspB1; HSPB1_HUMAN; SRP27; Stress responsive protein 27; Stress-responsive protein 27;
抗原和靶标
Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle.
- P04792 HSPB1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK
翻译修饰 - P04792 作为底物
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| R5 | Methylation | Uniprot | |
| S9 | Phosphorylation | Uniprot | |
| R12 | Methylation | Uniprot | |
| S15 | Phosphorylation | P49137 (MAPKAPK2) , Q05655 (PRKCD) , Q8IW41 (MAPKAPK5) , Q13976-2 (PRKG1) , Q16644 (MAPKAPK3) , P23443 (RPS6KB1) | Uniprot |
| Y23 | Phosphorylation | Uniprot | |
| S26 | Phosphorylation | Uniprot | |
| R37 | Methylation | Uniprot | |
| Y54 | Phosphorylation | Uniprot | |
| R56 | Methylation | Uniprot | |
| S65 | Phosphorylation | Uniprot | |
| Y73 | Phosphorylation | Uniprot | |
| S74 | Phosphorylation | Uniprot | |
| S78 | Phosphorylation | Q13237 (PRKG2) , Q13976 (PRKG1) , P23443 (RPS6KB1) , P17612 (PRKACA) , Q9UBS0 (RPS6KB2) , Q16644 (MAPKAPK3) , P49137 (MAPKAPK2) , Q8IW41 (MAPKAPK5) , P51812 (RPS6KA3) | Uniprot |
| S82 | Phosphorylation | P23443 (RPS6KB1) , P17612 (PRKACA) , Q8IW41 (MAPKAPK5) , P51812 (RPS6KA3) , P98161 (PKD1) , P49137 (MAPKAPK2) , Q9Y243 (AKT3) , Q9UBS0 (RPS6KB2) , Q13976 (PRKG1) , Q13237 (PRKG2) , P31751 (AKT2) , P31749 (AKT1) , Q16644 (MAPKAPK3) , Q15139 (PRKD1) | Uniprot |
| S83 | Phosphorylation | Uniprot | |
| S86 | Phosphorylation | Q05655 (PRKCD) | Uniprot |
| R89 | Methylation | Uniprot | |
| T91 | Phosphorylation | Uniprot | |
| S98 | Phosphorylation | Uniprot | |
| T110 | Phosphorylation | Uniprot | |
| K112 | Ubiquitination | Uniprot | |
| T113 | Phosphorylation | Uniprot | |
| K114 | Sumoylation | Uniprot | |
| K114 | Ubiquitination | Uniprot | |
| T121 | Phosphorylation | Uniprot | |
| K123 | Acetylation | Uniprot | |
| K123 | Ubiquitination | Uniprot | |
| Y133 | Phosphorylation | Uniprot | |
| S135 | Phosphorylation | Uniprot | |
| T139 | Phosphorylation | Uniprot | |
| K141 | Ubiquitination | Uniprot | |
| Y142 | Phosphorylation | Uniprot | |
| T143 | Phosphorylation | P17612 (PRKACA) , Q13976 (PRKG1) , Q13237 (PRKG2) | Uniprot |
| T162 | Phosphorylation | Uniprot | |
| T164 | Phosphorylation | Uniprot | |
| K171 | Ubiquitination | Uniprot | |
| T174 | Phosphorylation | Uniprot | |
| S176 | Phosphorylation | Q16539 (MAPK14) | Uniprot |
| T180 | Phosphorylation | Uniprot | |
| T184 | Phosphorylation | Uniprot | |
| S187 | Phosphorylation | Uniprot | |
| K198 | Sumoylation | Uniprot | |
| K198 | Ubiquitination | Uniprot | |
| S199 | Phosphorylation | Uniprot | |
| T202 | Phosphorylation | Uniprot | |
| K205 | Acetylation | Uniprot | |
| K205 | Ubiquitination | Uniprot |
研究背景
Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
Phosphorylated upon exposure to protein kinase C activators and heat shock. Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement.
Cytoplasm. Nucleus. Cytoplasm>Cytoskeleton>Spindle.
Note: Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle.
Homooligomer. Homodimer; becomes monomeric upon activation. Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin. Interacts with TGFB1I1 (By similarity). Interacts with CRYAB. Interacts with HSPB8. Interacts with HSPBAP1.
Belongs to the small heat shock protein (HSP20) family.
研究领域
· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)
· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
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