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.
引用格式: Affinity Biosciences Cat# AF5366, RRID:AB_2837851.
展开/折叠
78 kDa glucose regulated protein; 78 kDa glucose-regulated protein; AL022860; AU019543; BIP; D2Wsu141e; D2Wsu17e; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Endoplasmic reticulum lumenal Ca2+ binding protein grp78; Epididymis secretory sperm binding protein Li 89n; FLJ26106; Glucose Regulated Protein 78kDa; GRP 78; GRP-78; GRP78; GRP78_HUMAN; Heat shock 70 kDa protein 5; Heat Shock 70kDa Protein 5; Heat shock protein family A (Hsp70) member 5; HEL S 89n; Hsce70; HSPA 5; HSPA5; Immunoglobulin Heavy Chain Binding Protein; Immunoglobulin heavy chain-binding protein; mBiP; MIF2; Sez7;
抗原和靶标
- P11021 BIP_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL
种属预测
score>80的预测可信度较高,可尝试用于WB检测。*预测模型主要基于免疫原序列比对,结果仅作参考,不作为质保凭据。
High(score>80) Medium(80>score>50) Low(score<50) No confidence
翻译修饰 - P11021 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S4 | Phosphorylation | Uniprot | |
S14 | Phosphorylation | Uniprot | |
T37 | Phosphorylation | Uniprot | |
Y39 | Phosphorylation | Uniprot | |
R60 | Methylation | Uniprot | |
S64 | Phosphorylation | Uniprot | |
Y65 | Phosphorylation | Uniprot | |
T69 | O-Glycosylation | Uniprot | |
T69 | Phosphorylation | Uniprot | |
K81 | Ubiquitination | Uniprot | |
T85 | Phosphorylation | Uniprot | |
S86 | Phosphorylation | Uniprot | |
T91 | Phosphorylation | Uniprot | |
K96 | Acetylation | Uniprot | |
K96 | Ubiquitination | Uniprot | |
S107 | Phosphorylation | Uniprot | |
K113 | Acetylation | Uniprot | |
K113 | Ubiquitination | Uniprot | |
K118 | Acetylation | Uniprot | |
K118 | Ubiquitination | Uniprot | |
K122 | Acetylation | Uniprot | |
K123 | Acetylation | Uniprot | |
K123 | Ubiquitination | Uniprot | |
K125 | Acetylation | Uniprot | |
K125 | Ubiquitination | Uniprot | |
Y127 | Phosphorylation | Uniprot | |
K138 | Acetylation | Uniprot | |
K138 | Ubiquitination | Uniprot | |
T139 | Phosphorylation | Uniprot | |
S146 | Phosphorylation | Uniprot | |
K152 | Acetylation | Uniprot | |
K152 | Ubiquitination | Uniprot | |
K154 | Acetylation | Uniprot | |
K154 | Ubiquitination | Uniprot | |
Y160 | Phosphorylation | Uniprot | |
K163 | Acetylation | Uniprot | |
K163 | Ubiquitination | Uniprot | |
K164 | Ubiquitination | Uniprot | |
Y175 | Phosphorylation | Uniprot | |
K185 | Ubiquitination | Uniprot | |
T189 | Phosphorylation | Uniprot | |
R197 | Methylation | Uniprot | |
T203 | O-Glycosylation | Uniprot | |
T203 | Phosphorylation | Uniprot | |
Y209 | Phosphorylation | Uniprot | |
K213 | Ubiquitination | Uniprot | |
T229 | Phosphorylation | P11021 (HSPA5) | Uniprot |
K268 | Acetylation | Uniprot | |
K268 | Methylation | Uniprot | |
K268 | Ubiquitination | Uniprot | |
S311 | Phosphorylation | Uniprot | |
Y313 | Phosphorylation | Uniprot | |
S319 | Phosphorylation | Uniprot | |
K326 | Acetylation | Uniprot | |
K326 | Ubiquitination | Uniprot | |
K340 | Acetylation | Uniprot | |
K340 | Ubiquitination | Uniprot | |
K344 | Ubiquitination | Uniprot | |
K352 | Acetylation | Uniprot | |
K352 | Sumoylation | Uniprot | |
K352 | Ubiquitination | Uniprot | |
K353 | Acetylation | Uniprot | |
K353 | Sumoylation | Uniprot | |
K353 | Ubiquitination | Uniprot | |
S354 | Phosphorylation | Uniprot | |
S365 | Phosphorylation | Uniprot | |
T366 | Phosphorylation | Uniprot | |
K370 | Ubiquitination | Uniprot | |
K376 | Acetylation | Uniprot | |
K376 | Ubiquitination | Uniprot | |
K382 | Ubiquitination | Uniprot | |
T441 | Phosphorylation | Uniprot | |
K447 | Ubiquitination | Uniprot | |
S448 | Phosphorylation | Uniprot | |
S452 | Phosphorylation | Uniprot | |
T453 | Phosphorylation | Uniprot | |
S455 | Phosphorylation | Uniprot | |
T460 | Phosphorylation | Uniprot | |
K464 | Ubiquitination | Uniprot | |
Y466 | Phosphorylation | Uniprot | |
K474 | Ubiquitination | Uniprot | |
T485 | Phosphorylation | Uniprot | |
R492 | Methylation | Uniprot | |
T518 | Phosphorylation | Uniprot | |
K523 | Ubiquitination | Uniprot | |
T525 | Phosphorylation | Uniprot | |
T527 | Phosphorylation | Uniprot | |
K547 | Acetylation | Uniprot | |
K547 | Ubiquitination | Uniprot | |
S567 | Phosphorylation | Uniprot | |
Y568 | Phosphorylation | Uniprot | |
Y570 | Phosphorylation | Uniprot | |
S571 | Phosphorylation | Uniprot | |
K573 | Ubiquitination | Uniprot | |
K579 | Acetylation | Uniprot | |
K581 | Methylation | Uniprot | |
K585 | Acetylation | Uniprot | |
K585 | Methylation | Uniprot | |
K585 | Ubiquitination | Uniprot | |
S587 | Phosphorylation | Uniprot | |
S588 | Phosphorylation | Uniprot | |
K591 | Methylation | Uniprot | |
K596 | Methylation | Uniprot | |
K601 | Acetylation | Uniprot | |
K601 | Ubiquitination | Uniprot | |
S607 | Phosphorylation | Uniprot | |
K617 | Acetylation | Uniprot | |
K617 | Ubiquitination | Uniprot | |
K619 | Acetylation | Uniprot | |
S632 | Phosphorylation | Uniprot | |
K633 | Acetylation | Uniprot | |
K633 | Ubiquitination | Uniprot | |
Y635 | Phosphorylation | Uniprot | |
S637 | Phosphorylation | Uniprot | |
T643 | O-Glycosylation | Uniprot | |
T643 | Phosphorylation | Uniprot | |
T648 | Phosphorylation | Uniprot | |
K651 | Acetylation | Uniprot |
研究背景
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.
AMPylated by FICD. In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity).
Endoplasmic reticulum lumen. Melanosome. Cytoplasm.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Monomer and homooligomer; homooligomerization via the interdomain linker inactivates the chaperone activity and acts as a storage of HSPA5/BiP molecules (By similarity). Interacts with DNAJC1 (via J domain) (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity). Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Interacts with DNAJC10. Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1 (By similarity). Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity). Interacts with MX1 (By similarity). Interacts with METTL23. Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration. Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum. Interacts with CIPC. Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis. Interacts with INPP5K; necessary for INPP5K localization at the endoplasmic reticulum. Interacts with MANF; the interaction is direct. Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1 pathway of the unfolded protein response. Interacts with CLU under stressed condition; interaction increases CLU protein stability; facilitates its retrotranslocation and redistribution to the mitochondria; cooperatively suppress stress-induced apoptosis by stabilizing mitochondrial membrane integrity. Interacts with CCDC47 (By similarity).
The interdomain linker regulates the chaperone activity by mediating the formation of homooligomers. Homooligomers are formed by engagement of the interdomain linker of one HSPA5/BiP molecule as a typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP oligomerization inactivates participating HSPA5/BiP protomers. HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell. When the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers.
Belongs to the heat shock protein 70 family.
研究领域
· Genetic Information Processing > Folding, sorting and degradation > Protein export.
· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum. (View pathway)
· Human Diseases > Neurodegenerative diseases > Prion diseases.
· Organismal Systems > Immune system > Antigen processing and presentation. (View pathway)
· Organismal Systems > Endocrine system > Thyroid hormone synthesis.
文献引用
Application: WB Species: Mouse Sample:
Application: WB Species: Mice Sample: CD4+ T cells
Application: WB Species: Human Sample: HepG2 Cells
Application: WB Species: fish Sample:
Application: WB Species: Rat Sample:
Application: WB Species: Human Sample: KGN cells
Application: WB Species: rat Sample: spleen
Application: WB Species: Rat Sample: HSC-T6 cells
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