ライフサイエンスコーパス: llama

1 se submandibular glands induced ovulation in llamas.

2 nizing hormone (LH) release and ovulation in llamas.

3 m heavy chain antibodies found in camels and llamas.

4 odies obtained from lymphocytes of immunized llamas.

5 only antibodies, JM2 and JM4, from immunized llamas.

6 ally transported inland via caravans of pack llamas.

7 chain-only antibodies produced by camels and llamas.

8 Llamas adjusted their energy expenditure, Tb and locomot

9 Western blot analysis of llama and bull seminal plasma confirmed immunorecognitio

10 Camelid species (llama and camel) were selected for immunization because

11 Seminal plasma from llamas and bulls was used as representative of induced a

12 Llamas and camels were immunized with caffeine covalentl

13 d HIV-1 neutralization of a heavy chain-only llama antibody, named JM4.

14 ich are recombinantly derived from immunized llamas, are known to have high affinities for ricin A or

15 Cerro Azul itself did not raise llamas but obtained charqui (or dried meat) as well as o

16 -domain antibodies from camelids (camels and llamas) can circumvent both these obstacles.

17 Here, we describe two llama-derived single-domain antibodies (VHHs) that have

18 We assessed the efficacy of a llama-derived, heavy-chain antibody fragment called anti

19 of larger mammal bones such as bison, whale, llama, etc., the calibration curve showed a slower rate

20 oconstriction during acute hypoxaemia in the llama fetus is not mediated by stimulation of V1-vasopre

21 ictor tone in the femoral circulation in the llama fetus.

22 During saline infusion all llama fetuses responded to acute hypoxaemia with intense

23 Six llama fetuses were surgically prepared between 60 and 70

24 f granulocytic ehrlichiosis in a horse and a llama had recently occurred.

25 , is a 13-kDa soluble protein derived from a llama heavy chain antibody that binds with high affinity

26 TEC antibodies by fusing variable domains of llama heavy chain-only antibodies (VHHs) against ETEC to

27 ive library derived from variable regions of llama heavy chain-only antibodies, as fusions with a hyp

28 s was investigated using variable domains of llama heavy-chain antibodies (VHHs) as capture molecule,

29 ted a library of phage-displayed sdAb from a llama immunized with a cocktail of botulinum neurotoxin

30 able-domain repertoire library isolated from llamas immunized with recombinant CDTa or CDTb.

31 We created a phage display library from llamas immunized with ricin toxoid and selected a number

32 ia was identified in the blood of a diseased llama (lama glama).

33 Llamas (Lama glama) naturally produce heavy chain-only a

34 n is freely available to all users at http://llama.med.harvard.edu/funcassociate.

35 FuncAssociate is freely accessible at http://llama.med.harvard.edu/Software.html.

36 Please visit http://llama.med.harvard.edu/synergizer/doc for details.

37 For that purpose llamas (N = 7) were kept in a temperate habitat on pastu

38 Here, we produced and characterized llama nanobodies raised against the purified baseplate a

39 VWF:AF was determined using a llama nanobody (AU/VWFa-11) that detects a platelet-bind

40 A llama nanobody (AU/VWFa-11) that detects the mutant A1 d

41 the aim of the study was to determine if the llama, one of the most extensively kept domestic livesto

42 e domain antibody (nanobody) isolated from a llama phage display library that confers potent neutrali

43 Using a recently developed llama platform that generates human-like immunoglobulins

44 Llamas possess a class of unconventional immunoglobulins

45 d, yet were less sensitive than a comparable llama sdAb despite stemming from immune selections.

46 sdAbs, we constructed a large, semisynthetic llama sdAb library.

47 Thus, llamas seem to have maintained the ability to reduce the

48 A fraction isolated from llama seminal plasma by column chromatography was identi

49 e to fetal survival during hypoxaemia in the llama since their abolition leads to cardiovascular coll

50 In parallel we selected panels of llama single domain antibodies (sdAb) from a semi-synthe

51 synthetic phage display library of humanized llama single domain antibody (NaLi-H1: Nanobody Library

52 y for Marburg virus (MARV) that was based on llama single-domain antibodies (sdAbs) selected at biosa

53 ly isolated by phenotypic panning of a naive llama single-domain antibody phage display library.

54 hibitors, we created a library of non-immune llama single-domain VHH (camelid heavy-chain variable re

55 of ticks (Ixodes pacificus) collected at the llama site.

56 vy-chain-only antibody fragment (V(HH)) from llama that is capable of being utilized to analyze caffe

57 udy, a VHH phagemid library generated from a llama that was multiply immunized with recombinant trime

58 avy chain-only antibodies, JM2 and JM4, from llamas that have been immunized with a trimeric gp140 bo

59 )) chain variable domains, but in camels and llamas, the binding site frequently comprises the heavy

60 he study validates the utility of non-immune llama VHH libraries as a source of enzyme inhibitors and

61 ascular responses to acute hypoxaemia in the llama were investigated.

62 cattle, 25 horses, 57 sheep, 14 goats, and 1 llama were obtained and plated onto Enterococcosel agar

63 y library was generated by immunization of a llama with 4 human PCa cell lines.

64 After immunizing a llama with human PCSK9, we selected four sdAbs that bind