The present application is a U.S. National Phase application pursuant to 35 U.S.C. § 371 of International Application No. PCT/EP2014/054525 filed Mar. 10, 2014, which claims priority to European Patent Application No. 13158513.5 filed Mar. 11, 2013. The entire disclosure contents of these applications are herewith incorporated by reference into the present application.
Bearing component for a piston rod of a drug delivery device, piston rod comprising the bearing component, and drug delivery device.
Drug delivery devices, in particular pen-type injection devices, comprise a bung, which serves to eject doses of a drug from a container like a drug cartridge and may be provided as part of a drug cartridge. The bung is driven by a piston rod, which may be provided with a mechanism for setting a dose and for advancing the piston rod to deliver the dose set. In some pen-type injection devices the piston rod comprises a lead screw, which rotates when it is advanced during dose dispense. As a rotation of the bung is preferably avoided, there will be a relative rotation of the piston rod with respect to the bung during dispense. In this case a direct contact between the piston rod and the bung may result in large frictional losses and in a rather strong driving force being required. This disadvantage may be avoided by a suitable bearing. Furthermore, it is desirable to have a contact between the bung and the piston rod over as large an area as possible, because a small contact area or a point contact is liable to cause a deformation of the bung during dispense, thus reducing dose accuracy. Therefore a bearing component is preferably arranged between the piston rod and the bung. The bearing component can be formed to engage a large surface area of the bung and to contact only a small surface area of the piston rod, in order to facilitate a relative rotation of a component of the piston rod, like a lead screw, with respect to the bearing component. The bearing component must be able to assemble to the lead screw at relatively low assembly forces and without risking component damage. The bearing component must not become detached from the lead screw following assembly or during the device life, as this can result in dose inaccuracies. The bearing features must be robust enough to withstand the rigors of automated assembly and bulk packing.
US 2007/0093761 A1 discloses a drive mechanism suitable for use in drug delivery devices comprising a piston rod and a generally cylindrical drive sleeve surrounding the piston rod. A thread of the piston rod is adapted to work within a helical groove extending along the internal surface of the drive sleeve. A further thread of the piston rod extends through a threaded opening of an insert. A longitudinal axial movement of the drive sleeve causes the piston rod to rotate according to the thread of the insert, thereby advancing the piston rod and thus driving a piston in the cartridge. A bearing is provided on the piston rod by a pressure foot, which abuts the cartridge piston.
It is an object of the present invention to reduce frictional losses between a rotating piston rod and a bung for use in a drug delivery device.
This object is achieved with the bearing component according to claim 1, with the piston rod comprising the bearing component according to claim 8 and with the drug delivery device according to claim 12. Further embodiments derive from the dependent claims.
In one aspect the invention relates to a bearing component for a piston rod of a drug delivery device. The bearing component comprises a contact surface, a periphery, which surrounds a centre, and a coupling feature arranged inside the periphery for rotatably engaging a component of a piston rod perpendicular to the contact surface. The coupling feature includes a flexible feature extending from the periphery towards the centre, and the flexible feature is arranged to be deflected towards the periphery by a force exerted on the flexible feature in a direction towards the contact surface and deflected towards the centre by a force exerted on the flexible feature in the opposite direction. There may be only one flexible element, two flexible elements or more than two flexible elements.
In an embodiment of the bearing component, the flexible feature has sloping surfaces inclined with respect to the contact surface, the sloping surfaces approaching the contact surface towards the centre.
In a further embodiment the flexible feature is an integral part of the bearing component.
In a further embodiment the flexible feature is formed by at least one flexible arm, hook, prong, tooth or salient element.
In a further embodiment the centre comprises an opening, and the flexible feature limits the opening.
In a further embodiment the opening is enlarged when the flexible feature is deflected towards the periphery.
In a further embodiment the flexible feature is arranged such that the bearing component is symmetrical with respect to rotations by 180° around the centre.
In another aspect the invention relates to a piston rod comprising such a bearing component.
In an embodiment of the piston rod, the component of the piston rod that is rotatably engaged by the flexible feature is a lead screw.
In a further embodiment of the piston rod, the component of the piston rod that is rotatably engaged by the flexible feature comprises a coupler having an overhanging flange, and the bearing component engages the coupler with the flexible feature stopping the flange.
In a further embodiment of the piston rod, the component of the piston rod that is rotatably engaged by the flexible feature contacts the bearing component at least in a contact area near the periphery of the bearing component.
In another aspect the invention relates to a drug delivery device comprising such a bearing component, which may be mounted to a component of a piston rod. The drug delivery device may be an injection device, a pen-type device, and especially a pen-type injection device.
The term “drug”, as used herein, preferably means a pharmaceutical formulation containing at least one pharmaceutically active compound,
wherein in one embodiment the pharmaceutically active compound has a molecular weight up to 1500 Da and/or is a peptide, a proteine, a polysaccharide, a vaccine, a DNA, a RNA, an enzyme, an antibody or a fragment thereof, a hormone or an oligonucleotide, or a mixture of the above-mentioned pharmaceutically active compound,
wherein in a further embodiment the pharmaceutically active compound is useful for the treatment and/or prophylaxis of diabetes mellitus or complications associated with diabetes mellitus such as diabetic retinopathy, thromboembolism disorders such as deep vein or pulmonary thromboembolism, acute coronary syndrome (ACS), angina, myocardial infarction, cancer, macular degeneration, inflammation, hay fever, atherosclerosis and/or rheumatoid arthritis,
wherein in a further embodiment the pharmaceutically active compound comprises at least one peptide for the treatment and/or prophylaxis of diabetes mellitus or complications associated with diabetes mellitus such as diabetic retinopathy,
wherein in a further embodiment the pharmaceutically active compound comprises at least one human insulin or a human insulin analogue or derivative, glucagon-like peptide (GLP-1) or an analogue or derivative thereof, or exendin-3 or exendin-4 or an analogue or derivative of exendin-3 or exendin-4.
Insulin analogues are for example Gly(A21), Arg(B31), Arg(B32) human insulin; Lys(B3), Glu(B29) human insulin; Lys(B28), Pro(B29) human insulin; Asp(B28) human insulin; human insulin, wherein proline in position B28 is replaced by Asp, Lys, Leu, Val or Ala and wherein in position B29 Lys may be replaced by Pro; Ala(B26) human insulin; Des(B28-B30) human insulin; Des(B27) human insulin and Des(B30) human insulin.
Insulin derivates are for example B29-N-myristoyl-des(B30) human insulin; B29-N-palmitoyl-des(B30) human insulin; B29-N-myristoyl human insulin; B29-N-palmitoyl human insulin; B28-N-myristoyl LysB28ProB29 human insulin; B28-N-palmitoyl-LysB28ProB29 human insulin; B30-N-myristoyl-ThrB29LysB30 human insulin; B30-N-palmitoyl-ThrB29LysB30 human insulin; B29-N-(N-palmitoyl-Y-glutamyl)-des(B30) human insulin; B29-N-(N-lithocholyl-Y-glutamyl)-des(B30) human insulin; B29-N-(ω-carboxyheptadecanoyl)-des(B30) human insulin and B29-N-(ω-carboxyheptadecanoyl) human insulin.
Exendin-4 for example means Exendin-4(1-39), a peptide of the sequence H-His-Gly-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn-Gly-Gly-Pro-Ser- Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.
Exendin-4 derivatives are for example selected from the following list of compounds:
H-(Lys)4-des Pro36, des Pro37 Exendin-4(1-39)-NH2,
H-(Lys)5-des Pro36, des Pro37 Exendin-4(1-39)-NH2,
des Pro36 Exendin-4(1-39),
des Pro36 [Asp28] Exendin-4(1-39),
des Pro36 [IsoAsp28] Exendin-4(1-39),
des Pro36 [Met(O)14, Asp28] Exendin-4(1-39),
des Pro36 [Met(O)14, IsoAsp28] Exendin-4(1-39),
des Pro36 [Trp(O2)25, Asp28] Exendin-4(1-39),
des Pro36 [Trp(O2)25, IsoAsp28] Exendin-4(1-39),
des Pro36 [Met(O)14 Trp(O2)25, Asp28] Exendin-4(1-39),
des Pro36 [Met(O)14 Trp(O2)25, IsoAsp28] Exendin-4(1-39); or
des Pro36 [Asp28] Exendin-4(1-39),
des Pro36 [IsoAsp28] Exendin-4(1-39),
des Pro36 [Met(O)14, Asp28] Exendin-4(1-39),
des Pro36 [Met(O)14, IsoAsp28] Exendin-4(1-39),
des Pro36 [Trp(O2)25, Asp28] Exendin-4(1-39),
des Pro36 [Trp(O2)25, IsoAsp28] Exendin-4(1-39),
des Pro36 [Met(O)14 Trp(O2)25, Asp28] Exendin-4(1-39),
des Pro36 [Met(O)14 Trp(O2)25, IsoAsp28] Exendin-4(1-39),
wherein the group -Lys6-NH2 may be bound to the C-terminus of the Exendin-4 derivative;
or an Exendin-4 derivative of the sequence
des Pro36 Exendin-4(1-39)-Lys6-NH2 (AVE0010),
H-(Lys)6-des Pro36 [Asp28] Exendin-4(1-39)-Lys6-NH2,
des Asp28 Pro36, Pro37, Pro38Exendin-4(1-39)-NH2,
H-(Lys)6-des Pro36, Pro38 [Asp28] Exendin-4(1-39)-NH2,
H-Asn-(Glu)5des Pro36, Pro37, Pro38 [Asp28] Exendin-4(1-39)-NH2,
des Pro36, Pro37, Pro38 [Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-(Lys)6-des Pro36, Pro37, Pro38 [Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-Asn-(Glu)5-des Pro36, Pro37, Pro38 [Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-(Lys)6-des Pro36 [Trp(O2)25, Asp28] Exendin-4(1-39)-Lys6-NH2,
H-des Asp28 Pro36, Pro37, Pro38 [Trp(02)25] Exendin-4(1-39)-NH2,
H-(Lys)6-des Pro36, Pro37, Pro38 [Trp(O2)25, Asp28] Exendin-4(1-39)-NH2,
H-Asn-(Glu)5-des Pro36, Pro37, Pro38 [Trp(O2)25, Asp28] Exendin-4(1-39)-NH2,
des Pro36, Pro37, Pro38 [Trp(O2)25, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-(Lys)6-des Pro36, Pro37, Pro38 [Trp(O2)25, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-Asn-(Glu)5-des Pro36, Pro37, Pro38 [Trp(O2)25, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-(Lys)6-des Pro36 [Met(O)14, Asp28] Exendin-4(1-39)-Lys6-NH2,
des Met(O)14 Asp28 Pro36, Pro37, Pro38 Exendin-4(1-39)-NH2,
H-(Lys)6-desPro36, Pro37, Pro38 [Met(O)14, Asp28] Exendin-4(1-39)-NH2,
H-Asn-(Glu)5-des Pro36, Pro37, Pro38 [Met(O)14, Asp28] Exendin-4(1-39)-NH2,
des Pro36, Pro37, Pro38 [Met(O)14, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-(Lys)6-des Pro36, Pro37, Pro38 [Met(O)14, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-Asn-(Glu)5 des Pro36, Pro37, Pro38 [Met(O)14, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-Lys6-des Pro36 [Met(O)14, Trp(O2)25, Asp28] Exendin-4(1-39)-Lys6-NH2,
H-des Asp28 Pro36, Pro37, Pro38 [Met(O)14, Trp(02)25] Exendin-4(1-39)-NH2,
H-(Lys)6-des Pro36, Pro37, Pro38 [Met(O)14, Asp28] Exendin-4(1-39)-NH2,
H-Asn-(Glu)5-des Pro36, Pro37, Pro38 [Met(O)14, Trp(O2)25, Asp28] Exendin-4(1-39)-NH2,
des Pro36, Pro37, Pro38 [Met(O)14, Trp(O2)25, Asp28] Exendin-4(1-39)-(Lys)6-NH2,
H-(Lys)6-des Pro36, Pro37, Pro38 [Met(O)14, Trp(O2)25, Asp28] Exendin-4(S1-39)-(Lys)6-NH2,
H-Asn-(Glu)5-des Pro36, Pro37, Pro38 [Met(O)14, Trp(O2)25, Asp28] Exendin-4(1-39)-(Lys)6-NH2;
or a pharmaceutically acceptable salt or solvate of any one of the afore-mentioned Exendin-4 derivative.
Hormones are for example hypophysis hormones or hypothalamus hormones or regulatory active peptides and their antagonists as listed in Rote Liste, ed. 2008, Chapter 50, such as Gonadotropine (Follitropin, Lutropin, Choriongonadotropin, Menotropin), Somatropine (Somatropin), Desmopressin, Terlipressin, Gonadorelin, Triptorelin, Leuprorelin, Buserelin, Nafarelin, Goserelin.
A polysaccharide is for example a glucosaminoglycane, a hyaluronic acid, a heparin, a low molecular weight heparin or an ultra low molecular weight heparin or a derivative thereof, or a sulphated, e.g. a poly-sulphated form of the above-mentioned polysaccharides, and/or a pharmaceutically acceptable salt thereof. An example of a pharmaceutically acceptable salt of a poly-sulphated low molecular weight heparin is enoxaparin sodium.
Antibodies are globular plasma proteins (˜150 kDa) that are also known as immunoglobulins which share a basic structure. As they have sugar chains added to amino acid residues, they are glycoproteins. The basic functional unit of each antibody is an immunoglobulin (Ig) monomer (containing only one Igunit); secreted antibodies can also be dimeric with two Ig units as with IgA, tetrameric with four Ig units like teleost fish IgM, or pentameric with five Ig units, like mammalian IgM.
The Ig monomer is a “Y”-shaped molecule that consists of four polypeptide chains; two identical heavy chains and two identical light chains connected by disulfide bonds between cysteine residues. Each heavy chain is about 440 amino acids long; each light chain is about 220 amino acids long. Heavy and light chains each contain intrachain disulfide bonds which stabilize their folding. Each chain is composed of structural domains called Ig domains. These domains contain about 70-110 amino acids and are classified into different categories (for example, variable or V, and constant or C) according to their size and function. They have a characteristic immunoglobulin fold in which two β sheets create a “sandwich” shape, held together by interactions between conserved cysteines and other charged amino acids.
There are five types of mammalian Ig heavy chain denoted by α, δ, ϵ, γ, and μ. The type of heavy chain present defines the isotype of antibody; these chains are found in IgA, IgD, IgE, IgG, and IgM antibodies, respectively.
Distinct heavy chains differ in size and composition; α and γ contain approximately 450 amino acids and δ approximately 500 amino acids, while μ and ϵ have approximately 550 amino acids. Each heavy chain has two regions, the constant region (CH) and the variable region (VH). In one species, the constant region is essentially identical in all antibodies of the same isotype, but differs in antibodies of different isotypes. Heavy chains γ, α and δ have a constant region composed of three tandem Ig domains, and a hinge region for added flexibility; heavy chains μ and ϵ have a constant region composed of four immunoglobulin domains. The variable region of the heavy chain differs in antibodies produced by different B cells, but is the same for all antibodies produced by a single B cell or B cell clone. The variable region of each heavy chain is approximately 110 amino acids long and is composed of a single Ig domain.
In mammals, there are two types of immunoglobulin light chain denoted by λ and κ. A light chain has two successive domains: one constant domain (CL) and one variable domain (VL). The approximate length of a light chain is 211 to 217 amino acids. Each antibody contains two light chains that are always identical; only one type of light chain, κ or λ, is present per antibody in mammals.
Although the general structure of all antibodies is very similar, the unique property of a given antibody is determined by the variable (V) regions, as detailed above. More specifically, variable loops, three each the light (VL) and three on the heavy (VH) chain, are responsible for binding to the antigen, i.e. for its antigen specificity. These loops are referred to as the Complementarity Determining Regions (CDRs). Because CDRs from both VH and VL domains contribute to the antigen-binding site, it is the combination of the heavy and the light chains, and not either alone, that determines the final antigen specificity.
An “antibody fragment” contains at least one antigen binding fragment as defined above, and exhibits essentially the same function and specificity as the complete antibody of which the fragment is derived from. Limited proteolytic digestion with papain cleaves the Ig prototype into three fragments. Two identical amino terminal fragments, each containing one entire L chain and about half an H chain, are the antigen binding fragments (Fab). The third fragment, similar in size but containing the carboxyl terminal half of both heavy chains with their interchain disulfide bond, is the crystalizable fragment (Fc). The Fc contains carbohydrates, complement-binding, and FcR-binding sites. Limited pepsin digestion yields a single F(ab′)2 fragment containing both Fab pieces and the hinge region, including the H-H interchain disulfide bond. F(ab′)2 is divalent for antigen binding. The disulfide bond of F(ab′)2 may be cleaved in order to obtain Fab′. Moreover, the variable regions of the heavy and light chains can be fused together to form a single chain variable fragment (scFv).
Pharmaceutically acceptable salts are for example acid addition salts and basic salts. Acid addition salts are e.g. HCl or HBr salts. Basic salts are e.g. salts having a cation selected from alkali or alkaline, e.g. Na+, or K+, or Ca2+, or an ammonium ion N+(R1)(R2)(R3)(R4), wherein R1 to R4 independently of each other mean: hydrogen, an optionally substituted C1-C6-alkyl group, an optionally substituted C2-C6-alkenyl group, an optionally substituted C6-C10-aryl group, or an optionally substituted C6-C10-heteroaryl group. Further examples of pharmaceutically acceptable salts are described in “Remington's Pharmaceutical Sciences” 17. ed. Alfonso R. Gennaro (Ed.), Mark Publishing Company, Easton, Pa., U.S.A., 1985 and in Encyclopedia of Pharmaceutical Technology.
Pharmaceutically acceptable solvates are for example hydrates.
The following is a detailed description of embodiments of the bearing component and the piston rod comprising the bearing component in conjunction with the appended drawings.
The flexible features 8 of this embodiment have sloping surfaces 9, which are inclined with respect to the plane of the contact surface 2. The sloping surfaces 9 approach the contact surface 2 towards the centre 4, so that the coupling feature 5 grows narrower towards the plane of the contact surface 2. The flexible features 8 may be flexible arms, hooks, prongs, teeth or any other salient elements extending from the periphery 3 towards the centre 4. The flexible features 8 are preferably integral with the bearing component 1. The sloping surfaces 9 have the advantage that the assembly of the piston rod is facilitated, as will become apparent from the following description.
The flexible features 8 are preferably arranged within the outer ring 14 of the bearing component 1. The outer ring 14 protects the flexible features 8 from side loads that could arise if the device is subjected to impact or vibration or from direct loading on the component that might occur during an automated assembly or bulk transport situation. When the piston rod 7 is pushed towards the bung 15 during dispense, and the bearing component 1 is in compression, no load acts on the flexible features 8, so that the components 1, 6 stay securely coupled.
As shown in
Number | Date | Country | Kind |
---|---|---|---|
13158513 | Mar 2013 | EP | regional |
Filing Document | Filing Date | Country | Kind |
---|---|---|---|
PCT/EP2014/054525 | 3/10/2014 | WO | 00 |
Publishing Document | Publishing Date | Country | Kind |
---|---|---|---|
WO2014/139913 | 9/18/2014 | WO | A |
Number | Name | Date | Kind |
---|---|---|---|
533575 | Wilkens | Feb 1895 | A |
2895773 | McConnaughey | Jul 1959 | A |
4865591 | Sams | Sep 1989 | A |
5092842 | Bechtold et al. | Mar 1992 | A |
5226895 | Harris | Jul 1993 | A |
5226896 | Harris | Jul 1993 | A |
5279586 | Balkwill | Jan 1994 | A |
5304152 | Sams | Apr 1994 | A |
5320609 | Haber et al. | Jun 1994 | A |
5378233 | Haber et al. | Jan 1995 | A |
5383865 | Michel | Jan 1995 | A |
5391157 | Harris et al. | Feb 1995 | A |
5480387 | Gabriel et al. | Jan 1996 | A |
5505704 | Pawelka et al. | Apr 1996 | A |
5582598 | Chanoch | Dec 1996 | A |
5626566 | Petersen | May 1997 | A |
5674204 | Chanoch | Oct 1997 | A |
5688251 | Chanoch | Nov 1997 | A |
5688252 | Matsuda | Nov 1997 | A |
5735825 | Stevens | Apr 1998 | A |
5807346 | Frezza | Sep 1998 | A |
5820602 | Kovelman et al. | Oct 1998 | A |
5851079 | Horstman et al. | Dec 1998 | A |
5921966 | Bendek et al. | Jul 1999 | A |
5957896 | Bendek et al. | Sep 1999 | A |
5961495 | Walters et al. | Oct 1999 | A |
6004297 | Steenfeldt-Jensen et al. | Dec 1999 | A |
6193698 | Kirchhofer et al. | Feb 2001 | B1 |
6221046 | Burroughs et al. | Apr 2001 | B1 |
6235004 | Steenfeldt-Jensen et al. | May 2001 | B1 |
6248095 | Giambattista et al. | Jun 2001 | B1 |
6562006 | Hjertman et al. | May 2003 | B1 |
6613023 | Kirchhofer et al. | Sep 2003 | B2 |
6699224 | Kirchhofer et al. | Mar 2004 | B2 |
6899698 | Sams | May 2005 | B2 |
6932794 | Giambattista et al. | Aug 2005 | B2 |
6936032 | Bush, Jr. et al. | Aug 2005 | B1 |
7169132 | Bendek et al. | Jan 2007 | B2 |
7241278 | Moller | Jul 2007 | B2 |
7678084 | Judson et al. | Mar 2010 | B2 |
7850662 | Veasey et al. | Dec 2010 | B2 |
8186233 | Joung et al. | May 2012 | B2 |
20020052578 | Moller | May 2002 | A1 |
20020120235 | Enggaard | Aug 2002 | A1 |
20030050609 | Sams | Mar 2003 | A1 |
20040059299 | Moller | Mar 2004 | A1 |
20040097883 | Roe | May 2004 | A1 |
20040210199 | Atterbury et al. | Oct 2004 | A1 |
20040267207 | Veasey et al. | Dec 2004 | A1 |
20050113765 | Veasey et al. | May 2005 | A1 |
20060153693 | Fiechter et al. | Jul 2006 | A1 |
20070016143 | Miller et al. | Jan 2007 | A1 |
20070093761 | Veasey et al. | Apr 2007 | A1 |
20090275916 | Harms et al. | Nov 2009 | A1 |
20110319835 | Burren et al. | Dec 2011 | A1 |
20120136298 | Bendix | May 2012 | A1 |
20120265151 | Nzike et al. | Oct 2012 | A1 |
20130012888 | Okihara | Jan 2013 | A1 |
20130023831 | Helmer et al. | Jan 2013 | A1 |
20150151043 | Graf et al. | Jun 2015 | A1 |
Number | Date | Country |
---|---|---|
2138528 | Dec 1998 | CA |
2359375 | Jul 2000 | CA |
1547492 | Nov 2004 | CN |
1780652 | May 2006 | CN |
102448520 | May 2012 | CN |
102573961 | Jul 2012 | CN |
102821803 | Dec 2012 | CN |
0496141 | Jul 1992 | EP |
0897729 | Feb 1999 | EP |
0937471 | Aug 1999 | EP |
0937476 | Aug 1999 | EP |
1776975 | Apr 2007 | EP |
2438949 | Apr 2012 | EP |
2554204 | Feb 2013 | EP |
2008-538719 | Nov 2008 | JP |
2012-045173 | Mar 2012 | JP |
2012532720 | Dec 2012 | JP |
2132703 | Jul 1999 | RU |
9307922 | Apr 1993 | WO |
9324160 | Dec 1993 | WO |
WO 1994025090 | Nov 1994 | WO |
9938554 | Aug 1999 | WO |
0110484 | Feb 2001 | WO |
0230495 | Apr 2002 | WO |
02092153 | Nov 2002 | WO |
03080160 | Oct 2003 | WO |
2006084876 | Aug 2006 | WO |
WO 2006114396 | Nov 2006 | WO |
WO 2009039851 | Apr 2009 | WO |
WO 2010110712 | Sep 2010 | WO |
WO 2011006924 | Jan 2011 | WO |
2011042539 | Apr 2011 | WO |
WO-2011039229 | Apr 2011 | WO |
WO 2011121867 | Oct 2011 | WO |
Entry |
---|
Extended European Search Report issued in European Patent Application No. 13158513.5, dated Jul. 23, 2013. |
Examination Report issued in Australian Patent Application No. 2014230959 dated Jul. 29, 2017. |
“Pen-injectors for medical use—Part 1: Pen-injectors—Requirements and test methods,” International Standard, reference No. ISO 11608-1:2000(E), first edition Dec. 15, 2000, 32 pages. |
International Preliminary Report on Patentability in International Application No. PCT/EP2014/054525, dated Sep. 15, 2015, 7 pages. |
International Search Report and Written Opinion in International Application No. PCT/EP2014/054525, dated May 20, 2014, 11 pages. |
Number | Date | Country | |
---|---|---|---|
20160015901 A1 | Jan 2016 | US |