Recombinant Mouse Krev interaction trapped protein 1 (Krit1)

Code CSB-YP740859MO
MSDS
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Source Yeast
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Code CSB-EP740859MO
MSDS
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Source E.coli
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Code CSB-EP740859MO-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-BP740859MO
MSDS
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Source Baculovirus
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Code CSB-MP740859MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Krit1; Ccm1Krev interaction trapped protein 1; Krev interaction trapped 1; Cerebral cavernous malformations 1 protein homolog
Species
Mus musculus (Mouse)
Expression Region
1-736
Target Protein Sequence
MGNPENIEDA YVAVIRPKNT ASLNSREYRA KSYEILLHEV PIEGQKKKRK KVLLETKLQS NSEIAQGILD YVVETTKPIS PANQGIKGKR VVLMRKFPLD GEKTGREAAL FIVPSVVKDN TKYAYTPGCP IFYCLQDIMR VCSESSTHFA TLTARMLIAL DKWLDERHAQ SHFIPALFRP SPLERIKTNV INPAYAAELG QVDNSLHMGY SALEIKSKML ALEKADTCIY NPLFGSDLQY TNRVDKVVIN PYFGLGAPDY SKIQIPKQEK WQRSMSSVVE DKERQWVDDF PLHRNACEGD SELLSHLLDK GLSVNQLDND HWAPIHYACW YGKVEATRIL LEKGKCNPNL LNGQLSSPLH FAAGGGHAEI VQILLTHPDI DRHITDQQGR SPLNVCEENK QNNWEEAAKL LKDAINKPYE KVRIYRMDGS YRSVELKHGN NTTAQQIMEG MRLSQETQRY FTIWICSENL SLQFKPYHKP LQQVHDWPEI LAELTNLDPQ RETPQLFLRR DVGLPLEVEK KIEDPLAILI LFDEARYNLL KGFYTAPDAK LITLASLLLQ IVYGNYESKK HKQGFLNEET LKSIVPITKL KSKAPHWINR ILHEYKNLSL SEGVSKEMHH LQRMFLQNCW EIPTYGAAFF TGQIFTKASP SNHKVIPVYV GVNIKGLHLL NMETKALLIS LKYCCFTWQL GDAGTCFQIH SMENKMSFIV HTKQAGLVVK LLMKLNGQLM PSERNS
Protein Length
full length protein
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.
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
Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.
Gene References into Functions
  1. Data show that the reduced expression of thrombospondin1 (TSP1) that follows Krit1 inactivation contributes to cavernous malformation (CCM) lesion pathogenesis. PMID: 28970240
  2. Lesions develop in a stereotypic location and pattern, preceded by endothelial hypersprouting as confirmed in a zebrafish model of disease. The vascular defects seen with loss of Ccm1 suggest a defect in endothelial flow response. PMID: 24990152
  3. CCM1 silencing in endothelial cells caused decreased Notch3 activity in cocultured pericytes PMID: 25791711
  4. Data indicate that vascular endothelial growth factor (VEGF) signaling contributes to modifying endothelial function in Krev-interaction trapped 1 (KRIT1)-deficient cells and microvessel permeability in Krit1(+/-) mice. PMID: 25320085
  5. The CCM1 loss resulted in ICAP-1 destabilization, which increased beta1 integrin activation and led to increased RhoA-dependent contractility. PMID: 23918940
  6. Data indicate an integral role for KRIT1 in microvessel homeostasis and the vascular response to inflammation. PMID: 22922958
  7. Pdcd10 has a different role in cerebral cavernous malformation than Ccm2 and Krit1 PMID: 21490399
  8. Results suggests that KRIT1 limits the accumulation of intracellular oxidants and prevents oxidative stress-mediated cellular dysfunction and DNA damage by enhancing the cell capacity to scavenge intracellular ROS. PMID: 20668652
  9. The KRIT1-CCM2 interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA/ROCK signaling pathway. PMID: 20308363
  10. KRIT1 regulates beta-catenin signaling, and Krit1(+/-) mice are more susceptible to beta-catenin-driven intestinal adenomas. PMID: 20007487
  11. evidence of differential Krit1 and Rap1A expression during mouse ontogenesis and suggest a more widespread functional significance of Krit1, not restricted to vascular endothelial cells. PMID: 12172908
  12. Krit1 mRNA expression during mouse development from E7.5 to E20.5 and in adult tissues PMID: 12204286
  13. p53 plays a direct role in formation of cerebral vascular malformations by sensitizing mice with a mutation in Ccm1 (KRIT1) PMID: 15509522
  14. A familial CCM2 missense mutation abrogates the CCM1/CCM2 interaction, suggesting that loss of this interaction may be critical in cavernous malformations pathogenesis. PMID: 16037064
  15. CCM1 and CCM2 have similar expression patterns during development and are involved in the same pathway important for central nervous system vascular development PMID: 16373645
  16. The structure-function relationship of the C-terminal region of KRIT1A (cerebral cavernous malformations 1A protein) and the structural and functional impact of the 39 amino acid deletion characterizing the KRIT1B isoform was characterized. PMID: 18992740

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Subcellular Location
Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction.
Tissue Specificity
Expressed in heart, brain, spleen, lung, thymus, kidney and testis. Isoform 2 was more frequently expressed in the thymus than isoform 1.
Database Links
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