JPH0191776A - Culture medium - Google Patents
Culture mediumInfo
- Publication number
- JPH0191776A JPH0191776A JP62249621A JP24962187A JPH0191776A JP H0191776 A JPH0191776 A JP H0191776A JP 62249621 A JP62249621 A JP 62249621A JP 24962187 A JP24962187 A JP 24962187A JP H0191776 A JPH0191776 A JP H0191776A
- Authority
- JP
- Japan
- Prior art keywords
- human
- bcdf
- cell
- medium
- interleukin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 239000001963 growth medium Substances 0.000 title claims abstract 4
- 210000004027 cell Anatomy 0.000 claims abstract description 23
- 210000004408 hybridoma Anatomy 0.000 claims abstract description 10
- 102000004889 Interleukin-6 Human genes 0.000 claims abstract 6
- 108090001005 Interleukin-6 Proteins 0.000 claims abstract 6
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 5
- 239000002609 medium Substances 0.000 claims abstract 5
- 210000004102 animal cell Anatomy 0.000 claims abstract 4
- 210000003719 b-lymphocyte Anatomy 0.000 claims description 3
- 102000000646 Interleukin-3 Human genes 0.000 claims description 2
- 108010002386 Interleukin-3 Proteins 0.000 claims description 2
- 108090000623 proteins and genes Proteins 0.000 claims 3
- 108010071942 Colony-Stimulating Factors Proteins 0.000 claims 2
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 claims 2
- 102000000589 Interleukin-1 Human genes 0.000 claims 2
- 108010002352 Interleukin-1 Proteins 0.000 claims 2
- 102000000588 Interleukin-2 Human genes 0.000 claims 2
- 108010002350 Interleukin-2 Proteins 0.000 claims 2
- 102000004388 Interleukin-4 Human genes 0.000 claims 2
- 108090000978 Interleukin-4 Proteins 0.000 claims 2
- 102000000743 Interleukin-5 Human genes 0.000 claims 2
- 108010002616 Interleukin-5 Proteins 0.000 claims 2
- 229940028885 interleukin-4 Drugs 0.000 claims 2
- 229940100602 interleukin-5 Drugs 0.000 claims 2
- 239000006143 cell culture medium Substances 0.000 claims 1
- 230000010261 cell growth Effects 0.000 claims 1
- 239000003102 growth factor Substances 0.000 claims 1
- 229940076264 interleukin-3 Drugs 0.000 claims 1
- 238000010367 cloning Methods 0.000 abstract description 3
- 229920001184 polypeptide Polymers 0.000 abstract 2
- 108090000765 processed proteins & peptides Proteins 0.000 abstract 2
- 102000004196 processed proteins & peptides Human genes 0.000 abstract 2
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 abstract 1
- DPUOLKQSMYLRDR-UBHSHLNASA-N Phe-Arg-Ala Chemical compound NC(N)=NCCC[C@@H](C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 DPUOLKQSMYLRDR-UBHSHLNASA-N 0.000 abstract 1
- 102000007562 Serum Albumin Human genes 0.000 abstract 1
- 108010071390 Serum Albumin Proteins 0.000 abstract 1
- 210000002966 serum Anatomy 0.000 abstract 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 5
- 238000012258 culturing Methods 0.000 description 5
- 230000004663 cell proliferation Effects 0.000 description 4
- 230000035755 proliferation Effects 0.000 description 4
- 229940104230 thymidine Drugs 0.000 description 4
- 210000002798 bone marrow cell Anatomy 0.000 description 3
- MTHSVFCYNBDYFN-UHFFFAOYSA-N diethylene glycol Chemical compound OCCOCCO MTHSVFCYNBDYFN-UHFFFAOYSA-N 0.000 description 3
- 230000016784 immunoglobulin production Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 2
- 238000007447 staining method Methods 0.000 description 2
- VXJBRFHGOZMCOD-JURQXVEDSA-N 1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-2-methyloxolan-2-yl]-5-methyl-1,3-diazinane-2,4-dione Chemical compound C[C@@]1(C[C@H](O)[C@@H](CO)O1)N1C(=O)NC(=O)C(C)C1 VXJBRFHGOZMCOD-JURQXVEDSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 210000004128 D cell Anatomy 0.000 description 1
- 238000011765 DBA/2 mouse Methods 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 101001033276 Mus musculus Interleukin-3 Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241001499740 Plantago alpina Species 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 229910001632 barium fluoride Inorganic materials 0.000 description 1
- 238000004820 blood count Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000000663 muscle cell Anatomy 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
Description
【発明の詳細な説明】
ヒトＢリンツヤ腫ＢＡＬＬ−１ａ施を初発密度２Ｘ１０
’個／ｄとなるよう０．１ ％ ＢＳＡ （牛血清アル
ブミン含有ＡＳＦ １０３培地（販売人 味の素株式会
社）に懸濁し、最終濃度０−１０００ ｎｉ／ＩＩＩと
なるようと） ＢＣＤＦ ｆ：ｍ加し、ファルコン３０
２４７ ？スコ（２５ｉｕ）にて４日間、５チｃｏ２．
３７℃条件下で培養し喪、尚、この実験ではヒト ＢＣ
ＤＦとしてはヒト人１ａ−ＢＣＤＰを用いた。培養後各
々の生細胞密度をエオシン染色法によシ血球針算盤にて
計測した。また、培養上清中のヒトＩｇＭ抗体生産量を
ＥＬＩ８ム法にて計測した。[Detailed description of the invention] Human B lymphoma BALL-1a treated with initial density 2X10
0.1% BSA (suspended in ASF 103 medium containing bovine serum albumin (seller: Ajinomoto Co.) to give a final concentration of 0-1000 ni/III) BCDF f:m , Falcon 30
247? 4 days at Sco (25iU), 5chi CO2.
In this experiment, human BC was cultured at 37°C.
Human 1a-BCDP was used as DF. After culturing, the density of each living cell was measured using an eosin staining method using a blood cell count. Furthermore, the amount of human IgM antibody produced in the culture supernatant was measured by the ELI8 method.
結Ｍｔ−１通常（０１０％ ＦＢＳ添加ＲＰＭ１１６４
０ 培地を対照培地として用いた結果と比較し、第１図
に示した。Mt-1 normal (010% FBS added RPM1164
The results are shown in FIG. 1 in comparison with the results using the 0 medium as a control medium.
また無蛋白培地ム５Ｆ１０４培地（味の素社製）ＫＯＮ
１００ｎルーのと） ＢＣＤＦを添加し、初発細胞密度
５Ｘ１Ｇ’にてマウスハイブリドーマＳＳＩ［胞を５日
間培養後、各々の細胞密度を計測した結果を第２図に示
した。尚、この場合もヒト ＢＣＤＦとしてヒトＡ１畠
−ＢＣＤＦを用い丸。In addition, protein-free medium 5F104 medium (manufactured by Ajinomoto Co., Ltd.) KON
After culturing mouse hybridoma SSI cells for 5 days at an initial cell density of 5 x 1 G' with the addition of BCDF (100 n Roux), the cell density of each cell was measured, and the results are shown in Figure 2. In this case as well, human A1 Hatake-BCDF was used as human BCDF.
いずれの場合もヒト ＢＣＤＦ添加によシ、無添加に比
し細胞増殖及び抗体産生が促進された。In all cases, addition of human BCDF promoted cell proliferation and antibody production compared to the case without addition.
〔実施例２〕ヒト ＢＣＤＦを含有する培地での正常細
胞の増殖
マウス骨髄細胞を常法によＦｔ ＤＢＡ／２雌性マウス
よシ調製し、初発密度２．５Ｘ１０’個／ｍｌとなるよ
う２０％ＦＢＳ含有ＲＰＭ１１６４０培地に懸濁し、マ
ウスＩＬ−３（５Ｕ／Ｉｔｌ ）及び最終濃度０〜５０
ｎＶｄとなるようヒトＢＣＤＦを添加し、コーニング２
５８６０７’レー） （０，２ゴ）にて４日間、５チＣ
Ｏ２，３７℃条件下で培養し九。尚、この実験ではヒト
ＢＣＤＦとしてヒトＡｌａ−ＢＣＤＦを用いた。[Example 2] Proliferation of normal cells in a medium containing human BCDF Mouse bone marrow cells were prepared from Ft DBA/2 female mice by a conventional method, and diluted by 20% to give an initial density of 2.5 x 10' cells/ml. Suspended in RPM11640 medium containing FBS, mouse IL-3 (5 U/Itl) and final concentration 0-50
Add human BCDF to nVd, Corning 2
58607'Leh) (0,2go) for 4 days, 5chiC
Cultured under O2, 37°C conditions. In this experiment, human Ala-BCDF was used as human BCDF.
培養後各々の生細胞密度をエオシン染色法によシ血球計
算盤にて計測した。結果を第１表に示した。After culturing, the density of each viable cell was measured using an eosin staining method using a hemocytometer. The results are shown in Table 1.
通常培地では増殖維持困難な骨髄細胞がヒトＢＣＤＦ存
在下では維持された。またヒト ＢＣＤＦは第２のリン
ホカインマウスＩＬ−３と相乗作用を示し細胞を増殖さ
せた。Bone marrow cells, which are difficult to maintain proliferation in normal medium, were maintained in the presence of human BCDF. Human BCDF also showed synergistic effects with a second lymphokine, murine IL-3, to increase cell proliferation.
第１表
尚、生Ｎｉ廁密度はマウス骨髄細胞２．５Ｘ１０５／ｍ
ｔａｚ培地（２０％ ＦＢＳ含有ＲＰＭ１１６４０培地
）に懸濁し上記濃度のリンホカインを加えて４日間培養
後の生細胞密度である。In Table 1, the raw Ni density is 2.5 x 105/m for mouse bone marrow cells.
This is the density of viable cells after suspension in taz medium (RPM11640 medium containing 20% FBS), adding lymphokine at the above concentration, and culturing for 4 days.
ヒト ＢＣＤＦ ｉ＆はと）ＩｇＧを常法に従い免疫し
たマウスよ〕リンノダ節を採取した。このリッツ９筋細
胞１０２個とマウスミエローマ細胞Ｐ３．１０’個をＩ
ジエチレングリコール法にて細胞融合した後、Ｑ 〜Ｉ
ＱｎＪＦＪ＋ｊのヒトＢＣＤＦを加えたＨＡＴ （ヒポ
キサンチン・アミノグチリン・チミジン）培地中に希釈
して９６穴グレートにて３７℃、５％ＣＯ□条件下クロ
ーニングした。尚、この実施例で抗ヒト ＢＣＤＦ抗体
または抗と） ＩｇＧ抗体量をＥＬＩＳＡ法で測定した
。Rhynnoda nodes were collected from mice immunized with human BCDF i and IgG according to a conventional method. These 102 Ritz 9 muscle cells and P3.10' mouse myeloma cells were
After cell fusion using the diethylene glycol method, Q to I
QnJFJ+j was diluted in HAT (hypoxanthine-aminobutyline-thymidine) medium supplemented with human BCDF and cloned in a 96-well plate at 37°C under 5% CO□ conditions. In this example, the amount of anti-human BCDF antibody or anti-IgG antibody was measured by ELISA method.
添加したヒト ＢＣＤＦ １ｍ度、細胞の増殖したウェ
ルのｉ！−セント、目的のモノクローナル抗体を生産し
ているウェルの／譬−セントを第２表に示した。Added human BCDF 1 m degree, i! of the wells where the cells grew. Table 2 shows the number of wells producing the monoclonal antibody of interest.
第２表 ヒト ＢＣＤＦ添加培地での抗と） ＢＣＤＦ
抗体及び抗ヒトＩｇＧ抗体産生ハイブリドーマクローニ
ング効率の増強
〔実施例４〕ヒトＢＣＤＦ添加培地でのバイブリド９６
穴平底グレー）（０，２ｍｊ／ウェル）にて抗体産生ハ
イブリドーマ１００個／ウェルヲフィーダー細胞（Ｂａ
１ｂ／ ｃ ！ウス胸腺細胞５ Ｘ １０５個）ととも
にヒトＢＣＤＦ 、 Ｏ−１ｎｇｓを添加した培地Ｋ
ｌ！濁し九。３７℃５ ％ ＣＯ□条件下にて８日間培
養後、培養上清中の抗体量を酵素抗体法（ＢＩＪＳＡ）
Ｋて測定した。すなわち各ウェルの抗体の相対量を、ア
ルカリホスファターゼを結合したウサイ抗マウス免疫グ
ロブリン抗体に反応して分解したｐ−二ト四フェノール
ホスフェート量を示す４０５ｍｍでの吸光度で測定し、
４段階に区分しての全フェルに対する相対比および平均
値で示した。結果を第３表に示した。Table 2 Human anti-BCDF in BCDF-supplemented medium
Enhancement of antibody and anti-human IgG antibody producing hybridoma cloning efficiency [Example 4] Hybrid 96 in human BCDF-supplemented medium
100 antibody-producing hybridomas/well in feeder cells (Ba
1b/c! Medium K supplemented with human BCDF and O-1ngs (5 x 105 mouse thymocytes)
l! Cloudy nine. After culturing for 8 days at 37°C and 5% CO□, the amount of antibody in the culture supernatant was determined by enzyme-linked immunosorbent assay (BIJSA).
K was measured. That is, the relative amount of antibody in each well was measured by the absorbance at 405 mm, which indicates the amount of p-ditotetraphenol phosphate degraded in response to the alkaline phosphatase-conjugated bovine anti-mouse immunoglobulin antibody.
It is shown as a relative ratio and average value for all Fell divided into four stages. The results are shown in Table 3.
また同様の条件で抗体産生ハイブリドーマ５００個／ウ
ェルを３７℃ｓ １ ｃｏ、条件下にて７２時間あるい
は、１４４時間培讐した。それぞれ最後の８時間メチル
−（５Ｈ）−チミジンを０．５μＣ１／ウェル加え、細
胞に取〕込まれ九放射活性にて細胞の増殖能を測定した
。結果を第３図に示した。尚、本実施例で用いたヒト
ＢＣＤＦは辷ト人１ａ−ＢＣＤＦを用いた。Further, 500 antibody-producing hybridomas/well were cultured under the same conditions at 37° C. s 1 co for 72 hours or 144 hours. Methyl-(5H)-thymidine was added at 0.5 μC/well for the last 8 hours of each well, and the proliferative ability of the cells was measured based on the radioactivity taken up by the cells. The results are shown in Figure 3. In addition, the human used in this example
The BCDF used was the Totojin 1a-BCDF.
以上ヒト ＢＣＤＦはハイブリドーマの増殖、抗体産生
及びクローニング効率を促進した。As described above, human BCDF promoted hybridoma proliferation, antibody production, and cloning efficiency.
第３表
〔実施例５〕
！ウスＢ細胞ハイブリドーマＭＩ（６０、ＢａＦ２をＯ
〜０．２ ｍｌ ／ｒｒｔｌ ＢＣＤＦ ｆｔ＠有する
血清含有培地に５Ｘ １０’ 個／ａｔ（Ｄ細胞密［Ｉ
ＣＭ濁し、４２時ｒｍ培養し九、４２時間目に３Ｈ−チ
ミジンを添加し６時間後に細胞を集め、細胞の増殖を３
Ｈ−チミジンの取シこみで測定した。結果は第４図に示
した。Table 3 [Example 5]! murine B cell hybridoma MI (60, O BaF2
5X 10' cells/at (D cell density [I
Suspended in CM, cultured at 42 hours rm, added 3H-thymidine at 42 hours, collected cells 6 hours later, and inhibited cell proliferation for 3 hours.
It was measured by injecting H-thymidine. The results are shown in Figure 4.
ＢＣＤＦの添加量に相応して細胞の増殖は増加した。Cell proliferation increased in proportion to the amount of BCDF added.
なお、この実験ではヒト ＢＣＤＦとして天然屋ＢＣＤ
Ｆを用いた。In addition, in this experiment, Tennenya BCD was used as human BCDF.
F was used.
実施例で用いたＡＳＦ−１０３及びＡＳＦ−１０４の培
地組成を下記に示す。The medium compositions of ASF-103 and ASF-104 used in Examples are shown below.
第１図にはＢＡＬＬ−１細胞を初発密度２Ｘ１０５／ｄ
でＡ８Ｆ １０３培地（ＢＳＡ １〜／ｄ含有、ヒトＢ
ＣＤＦＯ〜１０００ ｎｊｌ添加）に懸濁し、４日培養
後の細胞密度と抗体産生量が示されている。
第２図には、８８−１細胞を初発密度５ Ｘ １０’／
ｄでλ８Ｆ １０４培地（ＢＳＡ無添加、ヒトＢＣＤＦ
Ｏ〜１００ ｎｌ／ｖｔｌ添加）ＫＭ濁し、５日培養
後の細胞密度が示されている。
第３図は抗体産生ハイブリドーマの増殖を３日目及び６
日目でのチミジンの取シ込み能で示した図である。
第４図はマウスＢ細胞ハイプリドーマの増殖を２日目で
のチミジン取シ込み能で示した図である。Figure 1 shows BALL-1 cells at an initial density of 2X105/d.
A8F 103 medium (BSA 1~/d containing, human B
The cell density and antibody production amount after 4 days of culture are shown. Figure 2 shows 88-1 cells at an initial density of 5 x 10'/
d in λ8F 104 medium (BSA-free, human BCDF)
The cell density after 5 days of culture is shown. Figure 3 shows the growth of antibody-producing hybridomas on days 3 and 6.
FIG. 3 is a diagram showing the ability to incorporate thymidine on days. FIG. 4 is a diagram showing the proliferation of mouse B cell hybridomas in terms of thymidine uptake ability on the second day.
Claims (1)
）を含有する動物細胞培養培地。（２）ヒトＢＣＤＦが
下記のアミノ酸配列（ I ）、（II）及び（III）のいず
れかである特許請求の範囲第（１）項記載の培地。 ￥アミノ酸配列（ I ）￥： 【遺伝子配列があります。】 ￥アミノ酸配列（II）￥： 【遺伝子配列があります。】￥アミノ酸配列（III）￥
：【遺伝子配列があります。】 （３）ヒトＢＣＤＦの濃度が０．０１〜１０００ｎｇ／
ｍｌである特許請求の範囲第（１）項記載の培地。 （４）動物細胞がヒト若しくはマウスの正常細胞、株化
細胞またはハイブリドーマである特許請求の範囲第（１
）項記載の培地。 （５）培地がインターロイキン１（ＩＬ−１）、インタ
ーロイキン２（ＩＬ−２）、インターロイキン３（ＩＬ
−３）、インターロイキン４（ＩＬ−４）、インターロ
イキン５（ＩＬ−５）、Ｂ細胞増殖因子（ＢＣＧＦ）及
びコロニー刺激因子（ＣＳＦ）のうち１種類以上を第２
のリンホカインとして含有するものである特許請求の範
囲第（１）項記載の培地。[Scope of Claims] (1) An animal cell culture medium containing human B cell differentiation factor (hereinafter referred to as human BCDF). (2) The culture medium according to claim (1), wherein the human BCDF has any of the following amino acid sequences (I), (II), and (III). ￥Amino acid sequence (I)￥: [There is a gene sequence. 】 ￥ Amino acid sequence (II) ￥: [There is a gene sequence. 】￥Amino acid sequence (III)￥
: [There is a gene sequence. (3) The concentration of human BCDF is 0.01 to 1000 ng/
ml of the medium according to claim (1). (4) Claim No. 1 in which the animal cells are human or mouse normal cells, established cell lines, or hybridomas.
) The medium described in section 2. (5) The medium is interleukin 1 (IL-1), interleukin 2 (IL-2), interleukin 3 (IL
-3), interleukin 4 (IL-4), interleukin 5 (IL-5), B cell growth factor (BCGF), and colony stimulating factor (CSF).
The culture medium according to claim (1), which contains the lymphokine as a lymphokine.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62249621A JPH0191776A (en) | 1987-10-02 | 1987-10-02 | Culture medium |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62249621A JPH0191776A (en) | 1987-10-02 | 1987-10-02 | Culture medium |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH0191776A true JPH0191776A (en) | 1989-04-11 |
Family
ID=17195750
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP62249621A Pending JPH0191776A (en) | 1987-10-02 | 1987-10-02 | Culture medium |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0191776A (en) |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS62263200A (en) * | 1986-05-08 | 1987-11-16 | イエダ リサ−チ アンド デベロツプメント コンパニ− リミテツド | Human interferon beta 2a and human interferon beta 2b, vector containing gene encoding said interferons, cell line producing the same and use thereof as drug |
-
1987
- 1987-10-02 JP JP62249621A patent/JPH0191776A/en active Pending
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS62263200A (en) * | 1986-05-08 | 1987-11-16 | イエダ リサ−チ アンド デベロツプメント コンパニ− リミテツド | Human interferon beta 2a and human interferon beta 2b, vector containing gene encoding said interferons, cell line producing the same and use thereof as drug |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Oi et al. | Immunoglobulin gene expression in transformed lymphoid cells. | |
| US5866689A (en) | Monoclonal antibodies to GP130 protein | |
| CN1871359B (en) | Methods of synthesizing heteromultimeric polypeptides in yeast using a haploid mating strategy | |
| Abrams et al. | Determination of the optimal human cell lines for development of human hybridomas. | |
| EP0327378B1 (en) | Domain-modified constant region antibodies | |
| JPH0686690A (en) | Method for producing antigen-specific human monoclonal antibody in vitro | |
| CN108640991B (en) | Antihuman interleukin 17A monoclonal antibody and its application | |
| US20040214289A1 (en) | Control of glycoforms in IgG | |
| EP0312996B1 (en) | Anti-human bcdf monoclonal antibody | |
| WO2002076578A1 (en) | Control of glycoforms in igg | |
| JPS59116231A (en) | Anti-interloykin-dimonoclonal antibody | |
| Strike et al. | Production of human-human hybridomas secreting antibody to sheep erythrocytes after in vitro immunization. | |
| EP0846169A1 (en) | MONOCLONAL ANTIBODIES AGAINST SOLUBLE TNF-ALPHA RECEPTORS p55 and p75 AS WELL AS AGAINST TNF-ALPHA AND ITS ANALOGUES | |
| JPH0191776A (en) | Culture medium | |
| Alter et al. | Variable globin chain synthesis in mouse erythroleukemia cells | |
| CN103827290A (en) | High-purity production of multi-subunit proteins such as antibodies in transformed microbes such as pichia pastoris | |
| WO1990002183A1 (en) | Production of a novel lymphokine exhibiting differentiation inhibitory activity | |
| Pavirani et al. | Recombinant proteins of therapeutic interest expressed by lymphoid cell lines derived from transgenic mice | |
| POSNER et al. | The generation of hybridomas secreting human monoclonal antibodies reactive with type II collagen | |
| Severinson et al. | IgG1 induction factor | |
| JP3043023B2 (en) | Hybridoma | |
| MXPA06004334A (en) | Methods of synthesizing heteromultimeric polypeptides in yeast using a haploid mating strategy | |
| EP0574461B2 (en) | High affinity humanized monoclonal antibodies | |
| Kawaguchi et al. | A monoclonal antibody against migration inhibitory factor (MIF) obtained by immunization with MIF from the human lymphoblast cell line Mo | |
| Olsson | Antibody producing human-human hybridomas |