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.
展开/折叠
Annexin A2; Annexin II; Annexin II, heavy chain; Annexin-2; ANX 2; ANX2; ANX2L4; ANXA2; ANXA2_HUMAN; arylsulfatase B; CAL1H; Calpactin I heavy chain; calpactin I heavy polypeptide (p36); Calpactin I heavy polypeptide; Calpactin-1 heavy chain; chromobindin 8; Chromobindin-8; Epididymis secretory protein Li 270; HEL S 270; LIP2; Lipocortin II; LPC2; LPC2D; p36; P36 protein; PAP-IV; Placental anticoagulant protein IV; Protein I;
抗原和靶标
A synthesized peptide derived from human Annexin A2, corresponding to a region within the internal amino acids.
- P07355 ANXA2_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
翻译修饰 - P07355 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Phosphorylation | Uniprot | |
T3 | Phosphorylation | Uniprot | |
K10 | Acetylation | Uniprot | |
K10 | Ubiquitination | Uniprot | |
S12 | Phosphorylation | P17252 (PRKCA) | Uniprot |
S18 | Phosphorylation | Uniprot | |
T19 | Phosphorylation | Uniprot | |
S22 | Phosphorylation | Uniprot | |
Y24 | Phosphorylation | P12931 (SRC) | Uniprot |
S26 | Phosphorylation | P05771 (PRKCB) , P17252 (PRKCA) | Uniprot |
K28 | Ubiquitination | Uniprot | |
Y30 | Phosphorylation | Uniprot | |
T31 | Phosphorylation | Uniprot | |
T44 | Phosphorylation | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
K49 | Acetylation | Uniprot | |
K49 | Sumoylation | Uniprot | |
K49 | Ubiquitination | Uniprot | |
T55 | Phosphorylation | Uniprot | |
T61 | Phosphorylation | Uniprot | |
Y75 | Phosphorylation | Uniprot | |
K81 | Ubiquitination | Uniprot | |
S85 | Phosphorylation | Uniprot | |
K88 | Ubiquitination | Uniprot | |
S89 | Phosphorylation | Uniprot | |
S92 | Phosphorylation | Uniprot | |
T97 | Phosphorylation | Uniprot | |
K104 | Acetylation | Uniprot | |
K104 | Ubiquitination | Uniprot | |
T105 | Phosphorylation | Uniprot | |
Y109 | Phosphorylation | Uniprot | |
S112 | Phosphorylation | Uniprot | |
K115 | Acetylation | Uniprot | |
K115 | Ubiquitination | Uniprot | |
S117 | Phosphorylation | Uniprot | |
K119 | Ubiquitination | Uniprot | |
T123 | Phosphorylation | Uniprot | |
S127 | Phosphorylation | Uniprot | |
C133 | S-Nitrosylation | Uniprot | |
S134 | Phosphorylation | Uniprot | |
T136 | Phosphorylation | Uniprot | |
Y147 | Phosphorylation | Uniprot | |
K148 | Acetylation | Uniprot | |
K148 | Ubiquitination | Uniprot | |
K152 | Acetylation | Uniprot | |
K152 | Ubiquitination | Uniprot | |
K157 | Acetylation | Uniprot | |
K157 | Ubiquitination | Uniprot | |
S161 | Phosphorylation | Uniprot | |
T163 | Phosphorylation | Uniprot | |
S164 | Phosphorylation | Uniprot | |
K169 | Methylation | Uniprot | |
K169 | Ubiquitination | Uniprot | |
K176 | Acetylation | Uniprot | |
K176 | Ubiquitination | Uniprot | |
S184 | Phosphorylation | Uniprot | |
Y188 | Phosphorylation | Uniprot | |
Y199 | Phosphorylation | Uniprot | |
K204 | Acetylation | Uniprot | |
K204 | Ubiquitination | Uniprot | |
K212 | Acetylation | Uniprot | |
K212 | Ubiquitination | Uniprot | |
S215 | Phosphorylation | Uniprot | |
T218 | Phosphorylation | Uniprot | |
S221 | Phosphorylation | Uniprot | |
K227 | Acetylation | Uniprot | |
K227 | Methylation | Uniprot | |
K227 | Ubiquitination | Uniprot | |
Y232 | Phosphorylation | Uniprot | |
K233 | Acetylation | Uniprot | |
K233 | Ubiquitination | Uniprot | |
S234 | Phosphorylation | Uniprot | |
Y235 | Phosphorylation | Uniprot | |
S236 | Phosphorylation | Uniprot | |
Y238 | Phosphorylation | Uniprot | |
S243 | Phosphorylation | Uniprot | |
K246 | Ubiquitination | Uniprot | |
K249 | Ubiquitination | Uniprot | |
C262 | S-Nitrosylation | Uniprot | |
K266 | Sumoylation | Uniprot | |
K266 | Ubiquitination | Uniprot | |
Y269 | Phosphorylation | Uniprot | |
Y275 | Phosphorylation | Uniprot | |
S277 | Phosphorylation | Uniprot | |
K279 | Acetylation | Uniprot | |
K279 | Ubiquitination | Uniprot | |
K281 | Ubiquitination | Uniprot | |
S296 | Phosphorylation | Uniprot | |
K302 | Acetylation | Uniprot | |
K302 | Ubiquitination | Uniprot | |
S305 | Phosphorylation | Uniprot | |
K310 | Acetylation | Uniprot | |
K313 | Acetylation | Uniprot | |
K313 | Methylation | Uniprot | |
K313 | Ubiquitination | Uniprot | |
S314 | Phosphorylation | Uniprot | |
Y316 | Phosphorylation | Uniprot | |
Y317 | Phosphorylation | Uniprot | |
Y318 | Phosphorylation | Uniprot | |
T323 | Phosphorylation | Uniprot | |
K324 | Acetylation | Uniprot | |
K324 | Sumoylation | Uniprot | |
K324 | Ubiquitination | Uniprot | |
K329 | Ubiquitination | Uniprot | |
Y333 | Phosphorylation | Uniprot |
研究背景
Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9.
Phosphorylation of Tyr-24 enhances heat stress-induced translocation to the cell surface.
ISGylated.
Secreted>Extracellular space>Extracellular matrix>Basement membrane. Melanosome.
Note: In the lamina beneath the plasma membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanism.
Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By similarity). Interacts with DYSF (By similarity). Interacts with COCH. Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal domain); the interaction inhibits the degradation of LDLR. Interacts with CEACAM1 (via the cytoplasmic domain); this interaction is regulated by phosphorylation of CEACAM1. Interacts with APPL2 and APPL1; targets APPL2 to endosomes and acting in parallel to RAB5A (By similarity).
(Microbial infection) Interacts with human cytomegalovirus (HCMV).
A pair of annexin repeats may form one binding site for calcium and phospholipid.
Belongs to the annexin family.
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