Certificate of Analysis and Data Sheet

Source:
Sf9 cells

Catalog No.
CYT-366

Background:

CTLA-4 is expressed in low copy number by T-cells only after activation, but it binds CD28-ligand with approximately 20-fold higher affinity than CD28. A soluble form of the extracellular domain of CTLA-4 has been shown to bind CD28-ligand with high avidity and to suppress T-cell-dependent antibody responses in vivo. Large doses of this soluble protein also suppress responses to a second immunization.

Description :

Recombinant Human CTLA-4 produced in insect cells is a homodimeric, glycosylated, polypeptide chain containing a total molecular mass of 80 kDa. Each subunit (40kDa) is fused to a polypeptide linker to the Fc portion of Human IgG1. CTLA-4 is expressed in low copy number by T-cells only after activation, but it binds CD28-ligand with approximately 20-fold higher affinity than CD28. A soluble form of the extracellular domain of CTLA-4 has been shown to bind CD28-ligand with high avidity and to suppress T-cell-dependent antibody responses in vivo.
Large doses of this soluble protein also suppress responses to a second immunization.
Recombinant Human CTLA-4 is purified by proprietary chromatographic techniques.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation:

Recombinant CTLA-4 was lyophilized with no additives.

Solubility:

It is recommended to reconstitute the lyophilized CTLA4 in sterile 18MΩ-cm H₂O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

Stability:

Lyophilized CTLA4 although stable at room temperature for 3 weeks, should be stored desiccated below -18⁰C. Upon reconstitution CTLA-4 should be stored at 4⁰C between 2-7 days and for future use below -18⁰C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

Amino acid sequence:

The sequence of the amino acids was determined and was found to be: Lys-Ala-Met-His-Val.

Dimers and aggregates:

Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Biological Activity:

ProSpec旧 Recombinant CTLA-4 is fully biologically active when compared to standards.

Endotoxin:

Less than 0.1 ng/ug (IEU/ug) of CTLA-4.

Protein content:

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280.
2. Analysis by RP-HPLC, using a standard solution of Human CTLA-4 as a Reference Standard.

Usage:

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Gene:

Name:CTLA4
Synonyms:CD152

Protein synonyms/aliases:

Cytotoxic T-lymphocyte protein 4 precursor (Cytotoxic T-lymphocyte-associated antigen 4)
    (CTLA-4)
    (CD152 antigen).

Protein Family:

Protein Domains:

Domains:

Protein links:

Precursor- Protein structure and amino acid sequence:

Latest Publications:

1. Polymorphisms at +49A/G and CT60 sites in the 3' UTR of the CTLA-4 gene and APECED-related AIRE gene mutations analysis in sporadic idiopathic hypoparathyroidism.
Int J Immunogenet 2005 Dec;32(6):393-400
2. Analysis of the cellular mechanism of antitumor responses and autoimmunity in patients treated with CTLA-4 blockade.
J Immunol 2005 Dec 1;175(11):7746-54
3. Estimation of diabetes risk in Brazilian population by typing for polymorphisms in HLA-DR-DQ, INS and CTLA-4 genes.
Dis Markers 2005;21(3):139-45
4. CTLA-4 and PD-1 receptors inhibit T-cell activation by distinct mechanisms.
Mol Cell Biol 2005 Nov;25(21):9543-53
5. Relationship between CTLA-4 and CD28 molecule expression on T lymphocytes and stimulating and blocking autoantibodies to the TSH-receptor in children with Graves' disease.
Horm Res 2005;64(4):189-97
6. CTLA-4 -1661A/G and -1772T/C dimorphisms in Japanese patients with systemic lupus erythematosus.
J Rheumatol 2005 Oct;32(10):2062

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中華民國95年06月06日更新