-
1
-
-
0030767656
-
Selection and identi fication of single domain antibody fragments from camel heavy-chain antibodies
-
Arbabi Ghahroudi M et al (1997) Selection and identi fication of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett 414:521-526
-
(1997)
FEBS Lett
, vol.414
, pp. 521-526
-
-
Arbabi Ghahroudi, M.1
-
2
-
-
0035715877
-
Single domain camel antibodies: Current status
-
Muyldermans S (2001) Single domain camel antibodies: current status. J Biotechnol 74:277-302
-
(2001)
J Biotechnol
, vol.74
, pp. 277-302
-
-
Muyldermans, S.1
-
3
-
-
70350787351
-
Ficoll-Paque™ versus Lymphoprep™: A comparative study of two density gradient media for therapeutic bone marrow mononuclear cell preparations
-
Yeo C, Saunders N, Locca D (2009) Ficoll-Paque™ versus Lymphoprep™: A comparative study of two density gradient media for therapeutic bone marrow mononuclear cell preparations. Regen Med 4:689-696
-
(2009)
Regen Med
, vol.4
, pp. 689-696
-
-
Yeo, C.1
Saunders, N.2
Locca, D.3
-
4
-
-
37549005602
-
Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in Escherichia coli
-
Olichon A, Surrey T (2007) Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in Escherichia coli. J Biol Chem 282: 36314-36320
-
(2007)
J Biol Chem
, vol.282
, pp. 36314-36320
-
-
Olichon, A.1
Surrey, T.2
-
5
-
-
52649114833
-
Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice
-
Garaicoechea L et al (2008) Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice. J Virol 82:753-764
-
(2008)
J Virol
, vol.82
, pp. 753-764
-
-
Garaicoechea, L.1
-
6
-
-
77951621074
-
Antibody-mediated puri fication of co-expressed antigen-antibody complexes
-
Bossi S et al (2010) Antibody-mediated puri fication of co-expressed antigen-antibody complexes. Protein Expr Purif 72:55-58
-
(2010)
Protein Expr Purif
, vol.72
, pp. 55-58
-
-
Bossi, S.1
-
7
-
-
78349296066
-
The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins
-
doi: 10.1155/2010/658954
-
Aliprandi M et al (2010) The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins. J Biomed Biotechnol. doi: 10.1155/2010/658954
-
(2010)
J Biomed Biotechnol
-
-
Aliprandi, M.1
-
8
-
-
65349172055
-
Immunological applications of single-domain llama recombinant antibodies isolated from a naive library
-
Monegal A et al (2009) Immunological applications of single-domain llama recombinant antibodies isolated from a naive library. Prot Engineer Des Sel 22:273-280
-
(2009)
Prot Engineer des Sel
, vol.22
, pp. 273-280
-
-
Monegal, A.1
-
9
-
-
0032559379
-
The specific variable domain of camel heavy-chain antibodies is encoded in the germline
-
Nguyen VK, Muyldermans S, Hamers R (1998) The specific variable domain of camel heavy-chain antibodies is encoded in the germline. J Mol Biol 275:413-418
-
(1998)
J Mol Biol
, vol.275
, pp. 413-418
-
-
Nguyen, V.K.1
Muyldermans, S.2
Hamers, R.3
-
10
-
-
0024292736
-
Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
-
Skerra A, Plückthun A (1988) Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240:1038-1041
-
(1988)
Science
, vol.240
, pp. 1038-1041
-
-
Skerra, A.1
Plückthun, A.2
-
11
-
-
77950022629
-
A single-domain llama antibody potently inhibits the enzymatic activity of Botulinum neurotoxin by binding to the non-catalytic a-exosite binding region
-
Dong J et al (2010) A single-domain llama antibody potently inhibits the enzymatic activity of Botulinum neurotoxin by binding to the non-catalytic a-exosite binding region. J Mol Biol 397:1106-1118
-
(2010)
J Mol Biol
, vol.397
, pp. 1106-1118
-
-
Dong, J.1
-
12
-
-
77954739350
-
A novel promiscuous class of camelid single-domain antibody contributes to the antigen-binding repertoire
-
Deschacht N et al (2010) A novel promiscuous class of camelid single-domain antibody contributes to the antigen-binding repertoire. J Immunol 184:5696-5704
-
(2010)
J Immunol
, vol.184
, pp. 5696-5704
-
-
Deschacht, N.1
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