Recombinant Human CAP-Gly domain-containing linker protein 1 (CLIP1), partial

Code CSB-YP005553HU
MSDS
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Source Yeast
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Code CSB-EP005553HU
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Source E.coli
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Code CSB-EP005553HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP005553HU
MSDS
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Source Baculovirus
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Code CSB-MP005553HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
CLIP1
Uniprot No.
Alternative Names
CAP GLY domain containing linker protein 1; CAP-Gly domain-containing linker protein 1; CLIP 170; CLIP; CLIP-170; CLIP1; CLIP1_HUMAN; CYLN1; cytoplasmic linker 1; Cytoplasmic linker protein 1; Cytoplasmic linker protein 170 alpha 2; Cytoplasmic linker protein 170 alpha-2; Cytoplasmic linker protein CLIP 170; Reed Steinberg cell expressed intermediate filament associated; Reed Sternberg intermediate filament associated protein 3; Reed-Sternberg intermediate filament-associated protein; Restin; RSN
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.
Gene References into Functions
  1. we report an unexpected finding that CLIP170 negatively regulates TLR4 signaling by the targeted ubiquitination and degradation of TIRAP. Furthermore, we observed that CLIP170 expression is modulated by LPS to maintain the cellular homeostasis. PMID: 29222167
  2. ASK1- induced phosphorylation of EB1 not only increases its plus end-tracking ability, but also promotes its recruitment of CLIP170 and p150glued to astral microtubules. PMID: 28039481
  3. single-molecule fluorescence microscopy showed that the microtubule plus-end-associated protein CLIP-170 binds tightly to formins to accelerate actin filament elongation. PMID: 27199431
  4. We find that LRRK1-mediated phosphorylation of CLIP-170 causes the accumulation of p150(Glued) (also known as DCTN1) a subunit of dynactin, at microtubule plus ends, thereby facilitating the migration of EGFR-containing endosomes. PMID: 25413345
  5. herpesvirus particles are absolutely dependent on CLIP-170-mediated capture to initiate transport in primary human cells. PMID: 26504169
  6. We show that AMPH-1/BIN1 binds to nesprin and actin, as well as to the microtubule-binding protein CLIP170 in both species. We propose that BIN1 has a direct and evolutionarily conserved role in nuclear positioning, altered in myopathies. PMID: 26506308
  7. Restin inhibits epithelial-mesenchymal transition and tumor metastasis by controlling the expression of the tumor metastasis suppressor mir-200a/b via association with p73. PMID: 25972084
  8. CLIP-170 tethers kinetochores to microtubule ends against the dynein-mediated poleward force to slide kinetochores along microtubules PMID: 26231764
  9. A defect in the CLIP1 gene (CLIP-170) can cause autosomal recessive intellectual disability. PMID: 24569606
  10. Data suggest that CLIP-170 acts as a novel recruiter and spatial regulator of PLK1 at kinetochores during early mitosis, promoting K-fiber stability and chromosome alignment for error-free chromosome segregation. PMID: 24777477
  11. siRNA-mediated knockdown of the cytoplasmic linker protein compromised the assembly and branching of capillary-like blood vessels and neovascularization in vivo. It was critical for the motility abilities of HUVECs through its actions on cell polarity. PMID: 24530770
  12. HDAC6 interacts with cytoplasmic linker protein 170 (CLIP-170) and that these two proteins function together to stimulate the migration of pancreatic cancer cells. PMID: 24474193
  13. CLIP-170 phosphorylation by Plk1 regulates proper chromosome alignment PMID: 24451569
  14. Depletion of CLIP-170 significantly impaired vascular endothelial tube formation and sprouting in vitro and inhibited breast tumor growth in mice by decreasing tumor vascularization. PMID: 23549612
  15. We further demonstrate that this binding was prevented when the C-terminal tyrosine of EB1 was absent in the peptidic probes. PMID: 22543185
  16. results suggest that EB1 and ClipCG12 act cooperatively to regulate microtubule dynamics (CLIP-170) PMID: 22424550
  17. End-binding proteins interact with the CAP-Gly domains of CLIP-170 and p150(glued). PMID: 22119847
  18. These results demonstrate that CLIP-170 mediates paclitaxel sensitivity in breast cancer via a microtubule-dependent mechanism. PMID: 21989536
  19. Herein, the authors have identified polo-like kinase 1 (Plk1) and casein kinase 2 (CK2) as two kinases of CLIP-170 and mapped S195 and S1318 as their respective phosphorylation sites. PMID: 20664522
  20. LIS1, CLIP-170's key to the dynein/dynactin pathway PMID: 11940666
  21. The cytoplasmic linker protein CLIP-170 is a human autoantigen PMID: 11966772
  22. Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170. PMID: 12110184
  23. expressed at high levels in monocyte-derived dendritic cells and IL-4 + CD40L-activated B cells and is involved in the trafficking of macropinosomes to the cytoskeleton, a crucial step in antigen presentation PMID: 12433698
  24. neogenin and restin have roles in proproliferation/survival action on ovarian cancer cells PMID: 12833147
  25. The restin gene was amplified from retinoic acid-treated promyelocytic cell line HL-60 by RT-PCR and cloned into a prokaryotic expression vector. PMID: 15862147
  26. these data explain observations that CLIP-170 localizes to newly polymerized microtubules in vitro but cannot track microtubule plus-ends in vitro. These observations have implications for the functions of CLIP-170 in regulating microtubule dynamics PMID: 16120651
  27. CLIP-170 facilitates the formation of kinetochore-microtubule attachments, possibly through direct capture of microtubules at the kinetochore. PMID: 16362039
  28. STAT-1alpha plays an important role in the atRA-induced transcriptional up-regulation of restin PMID: 16574066
  29. The function of CLIP-170 in membrane trafficking is not associated with plus-end localization. PMID: 16772339
  30. A structural basis for tubulin recognition by CLIP-170 and its autoinhibition is provided. PMID: 17563362
  31. Data use the complex formed between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle of CLIP170 as a model system to explore the structure-function relationship of CAP-Gly-mediated protein interactions. PMID: 17828277
  32. Crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces, are reported. PMID: 17889670
  33. The results suggest that promotion of lamellipodia formation and invasion by HGF or serum requires PI3K-dependent release of IQGAP1 and kinesin from Rac1-CLIP-170 complex. PMID: 18237546
  34. CLIP-170 was expressed in differentiated keratinocytes, first at the periphery of the nucleus then with a granular cytoplasmic labeling evocative of lamellar bodies PMID: 18622020
  35. Amphiphysin 2/BIN1 participates in the tubulation of traffic intermediates and intracellular organelles first via its intrinsic tubulating potential and second via its ability to bind CLIP-170 and microtubules. PMID: 19004523
  36. these results suggest that complexes of dynein, Lis1 and CLIP-170 crosslink and slide microtubules within the spindle, thereby producing an inward force that pulls centrosomes together. PMID: 19020519
  37. EB1 is both necessary and sufficient to mediate microtubule plus-end tracking by CLIP-170. PMID: 19126680
  38. Cdc2-mediated phosphorylation of CLIP-170 is essential for the normal function of this protein during cell cycle progression PMID: 19687009

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Subcellular Location
Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle.
Tissue Specificity
Detected in dendritic cells (at protein level). Highly expressed in the Reed-Sternberg cells of Hodgkin disease.
Database Links

HGNC: 10461

OMIM: 179838

KEGG: hsa:6249

STRING: 9606.ENSP00000303585

UniGene: Hs.524809

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