Recombinant Human C1GALT1-specific chaperone 1 (C1GALT1C1), partial

Code CSB-YP003490HU
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP003490HU
MSDS
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP003490HU-B
MSDS
Size Pls inquire
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.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP003490HU
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP003490HU
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
C1GALT1C1
Uniprot No.
Alternative Names
HSPC067; 3-galactosyltransferase 2; Beta 1,3 galactosyltransferase 2 ; Beta1,3 galactosyltransferase 2 ; C1Gal T2 ; C1Gal-T2; C1GALT1 specific chaperone 1 ; C1GALT1-specific chaperone 1; C1galt1c1; C1GalT2; C1GLC_HUMAN; C38H2 L1; C38H2 like protein 1; C38H2-L1; C38H2-like protein 1; C38H2L1; Core 1 beta1; Core 1 beta3 galactosyltransferase specific molecular chaperone; Core 1 beta3-Gal-T2; Core 1 beta3-galactosyltransferase-specific molecular chaperone; Core 1 UDP galactose:N acetylgalactosamine alpha R beta 1,3 galactosyltransferase 2 ; COSMC ; MGC19947; MST143
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.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
Probable chaperone required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3-galactosyltransferase (C1GALT1).
Gene References into Functions
  1. In addition, we found that Tn-expressing colorectal cancers (CRC) cell lines had either loss-of-function mutations in Cosmc or reversible Tn antigen expression, which was not caused by the deficiency of T-synthase activity PMID: 30115016
  2. elevated Tn levels in cancer and inflammation may be commonly regulated by the cytokine (TNFa and IL6)-Cosmc signaling axis PMID: 27542280
  3. The data suggest that hypermethylation of the Cosmc promoter may induce the expression of Tn antigen in activated T cells. PMID: 28708980
  4. results provide new structure-function insight to Cosmc, indicate that Cosmc behaves as a modular protein and suggests points of modulation or regulation of in vivo chaperone function PMID: 28665962
  5. Data indicate that mRNA levels of both core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1 (C1GALT1) and C1GALT1-specific chaperone 1 protein (C1GALT1C1) determine the rate of secretion of galactose-deficient IgA1 (Gd-IgA1) in IgA1-producing cells. PMID: 28187132
  6. The terminal glycosylation of secreted IgA1 was altered in response to TGFbeta1. TGFbeta1 stimulation significantly decreased the mRNA levels of C1GalT1 and Cosmc. TGFbeta1 may be key in controlling the glycosylation of IgA1, in part via the downregulation of C1GalT1 and Cosmc. PMID: 28035353
  7. mutations c.393T>A and c.72A>G in the exon region of Cosmc gene in children with Henoch-Schonlein purpura (HSP) are not associated with the onset of Henoch-Schonlein purpura PMID: 27412546
  8. Data suggest that patients with IgA nephropathy exhibit higher microRNA-374b in B cells compared to controls; microRNA-374b appears to target PTEN (phosphatase and tensin homolog) and Cosmc (C1GALT1 specific chaperone 1) proteins. PMID: 26545495
  9. These results indicate that Tn antigens expression and T-synthase inactivity in HT-29-Tn+ cells can be related to the absence of the Cosmc gene coding sequence in Cosmc active alleles PMID: 26045765
  10. the impact of COSMC mediated Tn antigen expression in two human pancreatic ductal adenocarcinoma cell lines on cellular oncogenic properties, were investigated. PMID: 26021314
  11. hypermethylation of Cosmc promoter region could be a key mechanism for the reduction of Cosmc mRNA expression in IgAN lymphocytes with associated increase in aberrantly glycosylated IgA1 PMID: 25647400
  12. Cosmc and T-synthase are transcriptionally regulated at a basal level by the specificity protein/Kruppel-like transcription factor family of members. PMID: 26063800
  13. CBRT is a unique recognition motif for Cosmc to promote its regulation and formation of active T-synthase and represents the first sequence-specific chaperone recognition system in the ER/Golgi required for normal protein O-glycosylation PMID: 24616093
  14. Data indicate that cytotoxin associated gene A protein (CagA) promoted the underglycosylation of IgA1, which at least partly attributed to the downregulation of beta1,3-galactosyltransferase (C1GALT1) and its chaperone Cosmc. PMID: 24462875
  15. overexpression of Cosmc is associated with colorectal cancer. PMID: 23390052
  16. COSMC is a novel regulator for VEGFR2 signaling in endothelial cells and dysregulation of COSMC expression may contribute to the pathogenesis of hemangioma PMID: 23424651
  17. The mRNA expression level of Cosmc gene in IgA nephropathy patients was significantly lower than that of controls. De-methylation modification up regulated the Cosmc gene expression significantly. PMID: 22332537
  18. Results show that soluble Cosmc directly interacts in a specific manner with denatured, but not native, T-synthase to form a noncovalent and reversible complex that results in the acquisition of T-synthase catalytic activity. PMID: 22416136
  19. Results indicate that Cosmc mediates the co-translational activation of C1GalT and that it may prevent the unfavorable aggregation of C1GalT. PMID: 21496458
  20. The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum PMID: 21262965
  21. Study results suggest that C1GALT1C1 may play a key role in the regulation of IgA1 O-glycosylation. PMID: 20144270
  22. Cosmc represents the first endoplasmic reticulum chaperone identified to be required for folding of a glycosyltransferase PMID: 19923218
  23. molecular cloning and characterization; C1Gal-T2 is the second candidate for core 1 synthase that plays an important role in synthesizing O-glycans in digestive organs PMID: 12361956
  24. Tn syndrome is associated with a somatic mutation in Cosmc, a gene on the X chromosome that encodes a molecular 'chaperone' that is required for the proper folding and hence full activity of T-synthase PMID: 16251947
  25. These results suggest that the intracellular dynamics of C1GalT is controlled by its specific molecular chaperon, Cosmc, in association with core 1 synthase activity. PMID: 18061573
  26. The tumor-specific antigen caused by mutant COSMC seems to be rare and is not potentially a therapeutic target candidate in breast and colon cancers. PMID: 18321367
  27. Colon cancer and melanoma-derived cells lines expressed Tn and STn antigen due to loss-of-function mutations in Cosmc. Cervical cancer specimens that showed expression of the Tn/STn antigens were also found to have mutations in Cosmc. PMID: 18339842
  28. a novel inactivating mutations (Glu152Lys, Ser193Pro and Met1Ile) in the coding sequence of C1GALT1C1 PMID: 18537974
  29. Cosmc is an endoplasmic reticulum (ER)-localized adenosine triphosphate binding chaperone that binds directly to human T-synthase. PMID: 18695044
  30. Although decreased C1GALT1 activity has been implicated in IgAN pathogenesis and cosmc chaperone mutations can cause autoimmune disease, our data provide no evidence for a role of cosmc gene mutations in European patients with sporadic or familial IgAN. PMID: 18840896
  31. The c.-347-190G>A polymorphism and the somatic mutation of encoding region of C1GALT1C1 gene were not significantly related to the genetic susceptibility to IgAN in Northern Chinese population PMID: 19778426

Show More

Hide All

Involvement in disease
Tn polyagglutination syndrome (TNPS)
Subcellular Location
Membrane; Single-pass type II membrane protein.
Protein Families
Glycosyltransferase 31 family, Beta3-Gal-T subfamily
Tissue Specificity
Ubiquitously expressed. Abundantly expressed in salivary gland, stomach, small intestine, kidney, and testis and at intermediate levels in whole brain, cerebellum, spinal cord, thymus, spleen, trachea, lung, pancreas, ovary, and uterus.
Database Links

HGNC: 24338

OMIM: 300611

KEGG: hsa:29071

STRING: 9606.ENSP00000304364

UniGene: Hs.643920

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1