United States Patent 9,914,785: Claim-Scope Deconstruction and US Patent Landscape

What is US 9,914,785 claiming at a technical level?

US 9,914,785 is directed to antibody constructs engineered to enforce correct heavy-chain/light-chain pairing in multi-antibody expression contexts. The core claim structure is a two-heterodimer system built from four polypeptide chains: two heavy chains (H1, H2) and two light chains (L1, L2). The constructive novelty is not the antigen specificity per se, but the pairing control created by specific Kabat-position amino-acid substitutions intended to bias heterodimer formation toward the intended cognate pairs.

Claim 1 anchor: two intended heterodimers plus pairing bias

Claim 1 recites an antibody construct comprising:

First heterodimer: H1 (IgG heavy chain with VH + CH1) + L1 (light chain with VL + CL)
Second heterodimer: H2 (IgG heavy chain with VH + CH1) + L2 (light chain with VL + CL)
H1/H2/L1/L2 each contain at least one substitution set selected from five families (a–e), each defined by Kabat numbering and limited to heavy-chain and light-chain residues.
The substitutions are selected to promote preferential pairing:
- H1 pairs with L1 more than with L2, and/or
- H2 pairs with L2 more than with L1 when co-expressed in a cell.

Substitution “families” in Claim 1 (Kabat positions)

Claim 1 lists five substitution families (conservative substitutions permitted). The families are:

(a)

H1: 146G, 179K
L1: 124E, 160E, 180E
H2: 143E, 145T
L2: 160K, 178R

(b)

H1: 143K, 146G
L1: 124E, 133D
H2: 143E, 145T
L2: 124R

(c)

H1: 146G, 179R
L1: 124E, 160E, 178D
H2: 145T, 179D, 188L
L2: 160K, 178R

(d)

H1: 143A, 146G, 179R
L1: 124E, 133W, 160E, 180E
H2: 145T, 179D, 188F
L2: 133A, 160K, 178R

(e)

H1: 146G, 186R
L1: 124E, 160E, 178D
H2: 145E, 146G, 179D, 188L
L2: 124R, 160K, 178R

Key legal implication: Claim 1 is not “any pairing mutation.” It is limited to these residue sets (and conservative equivalents) at defined Kabat positions. That tightness usually helps enforceability, but it can narrow commercial coverage if competitors choose alternative pairing mutations.

How do the dependent claims tighten scope beyond the mutation set?

What does Claim 2 add (kappa light chain requirement)?

Claim 2 limits L1 and/or L2 to kappa light chains.

Landscape impact: Many pairing systems are built across lambda and kappa formats. This claim narrows to the kappa subset, reducing overlap with lambda-centric antibody engineering.

What does Claim 3–4 require about Fc/IgG expression?

Claim 3: each heterodimer includes a full-length IgG heavy chain with an Fc domain.
Claim 4: the Fc domain of H1 preferentially interacts with the Fc domain of H2 relative to forming a homodimer.

Critical technical point: Claim 4 introduces another orthogonal pairing mechanism: Fc-Fc heterodimer preference. That can reduce mispairing at the Fc level, but it also increases design constraints (and potential infringement complexity if a product lacks Fc heterodimer engineering).

What does Claim 5 do (IgG subclass constraint)?

Claim 5: H1 and H2 are from IgG1, IgG2, IgG3, or IgG4.

Scope note: This leaves out IgA, IgM, and non-IgG scaffolds.

What does Claim 6 add (quantified heterodimer yield)?

Claim 6: when both light chains are co-expressed with at least one heavy chain (H1 and/or H2), the relative yield of correct heterodimer(s) exceeds the yield of mispaired heterodimer(s).
Threshold: greater than 50% relative yield for correct pairings vs corresponding mispairings.

Enforcement implication: Yield-based limitations can be harder to prove in litigation unless the patentee can tie the mutation set to that performance in the specification and the defendant’s product is tested under comparable expression conditions.

What does Claim 7 add (melting temperature constraint)?

Claim 7: Tm of at least one heterodimer is within about 10°C of the corresponding heterodimer without the substitutions.

Commercial consequence: Competitors can sometimes “work around” by using different substitutions that alter stability but still achieve pairing. This constraint narrows performance escape routes.

What does Claim 8 add (affinity retention constraint)?

Claim 8: affinity for each heterodimer’s antigen is within about 50-fold of wild type heterodimer affinity.

Legal consequence: If a competitor changes residues such that affinity retention is lower than this band, they likely avoid the claim even if they achieve pairing.

What does Claim 9 add (bispecific)?

Claim 9: the antibody construct is bispecific.

Landscape consequence: This frames the construct as at least a two-antigen or two-binding-site format. Many pairing systems are used in multispecifics beyond bispecific; this claim targets bispecific use cases more directly.

Claim 10 and Claim 11: the same invention, reshuffled mutation sets with different dependent geometry

Claim 10 repeats the two-heterodimer construct but lists the same overall structure with substitution families again (a–e). Claim 11 shifts from heterodimer format to a composition comprising a set of polypeptides (L1, L2, and H1), including additional specific mutation combinations and a preferential pairing requirement.

What does Claim 11 add (composition formulation plus different substitution combinations)?

Claim 11 lists explicit substitution combinations (a–j). It includes:

H1 variants with Kabat residues such as 143A/143E/143K, 145T/145E, 146G, 179K/179R/179D, 186R, and 188L/188F.
L1 variants with 124E/124R, 133D/133W/133A, 160E/160K, 178D/178R, 180E.
L2 variants with multiple residues, including 160K, 178R, 178D, 180E, etc.
A preferential pairing statement: H1 preferentially pairs with L1 as compared to L2 when co-expressed in a cell.

What does Claim 15 quantify further (55% yield threshold)?

Claim 15: relative yield of H1-L1 vs mispaired H1-L2 is > 55% when both L1 and L2 are co-expressed with H1.

Legal tightening: Claim 15 creates a higher performance ceiling than Claim 6’s 50% framework, raising the bar for infringement proof (or for reaching the claim’s dependent coverage).

Critical claim-analysis: where the patent is strong vs where it is fragile

1) The patent’s center of gravity is the residue-set-controlled pairing

The claims do not require any particular antigen epitope or binding site sequences. Instead, they require specific Kabat-position amino-acid substitutions that create differential pairing.

Strength: residue-set specificity is easier to match against a competitor’s sequence if you have the chain sequences.

Fragility: if a competitor uses alternative pairing mutations at different Kabat positions, they likely avoid literal coverage even if the product achieves pairing via other mechanisms (electrostatics, sterics, CH1-VL interface redesign, or Fc-based pairing).

2) The “conservative substitutions” language increases ambiguity

Each family allows “conservative substitutions thereof.” That can expand literal scope, but it also injects interpretive risk. Conservativeness depends on definition and expert testimony.

Enforcement impact: it can help the patentee capture near-miss designs, but it also complicates predictability for clearance.

3) Performance limits (yield, Tm, affinity) can become either strong anchors or litigation friction

Yield > 50% or > 55%
Tm within about 10°C
Affinity within about 50-fold

If the specification contains strong in vitro and cell expression data showing these exact bounds for the listed mutation sets, these limitations become potent for invalidity defense (and for infringement proof). If data are thin or conditions differ, they can weaken enforceability through “not met” arguments.

4) Fc pairing (Claim 4) adds a second axis that may be absent in many products

Even if a bispecific product uses H/L pairing mutations, it may not engineer Fc heterodimer preference. If Claim 4 is asserted, absence of Fc-Fc engineering can be a clean non-infringement path.

5) IgG subclass constraint still permits wide real-world usage

IgG1–IgG4 are covered. Many therapeutic platforms heavily use IgG1, and a large fraction of bispecifics remain in IgG1. This broad subclass coverage reduces design-out opportunities based solely on subclass.

Where does this sit in the broader pairing and multispecific antibody landscape?

Functional problem addressed: wrong chain pairing in multi-antibody co-expression

In multi-antibody expression (including bispecifics and other multi-specific constructs), heavy-light mispairing reduces product yield and can create heterogeneity. The standard industry toolbox includes:

mutation at the VH-VL/CH1-CL interface
engineered charge/shape complementarity
orthogonal CH1/CL interfaces
knob-into-hole-like or Fc-Fc heterodimer engineering (for heavy-heavy pairing)
additional stabilizing mutations to avoid affinity or stability loss

US 9,914,785’s claims are most aligned with the interface mutation strategy, and partially with Fc-Fc heterodimerization when Claim 4 is asserted.

Competitive design-around vectors likely to matter

Because the claims are residue-set bounded by Kabat positions, the most plausible workarounds are:

substitute different Kabat-position residues at the CH1-CL interface
use different frameworks with pairing mutations outside these listed positions
rely on non-Cabal-disclosed mechanisms like “proximity” formats or platform-specific orthogonality where pairing is not achieved by the specified substitutions
avoid any engineered Fc heterodimer interactions so Claim 4 cannot attach

What does the patent landscape look like (US) for this concept?

Which earlier US patents are most likely to overlap with US 9,914,785?

A full, accurate US landscape requires identifying the patent family of US 9,914,785 (priority dates, applicants, and cited prior art in the prosecution history). The user provided only the claims text and not the bibliographic record, publication identifiers, prosecution citations, or assignee/priority.

With that missing, it is not possible to produce a complete and accurate set of overlapping US patent documents, nor to map claim charts across likely incumbents and design platforms.

Which assignee and technology context matters for a defensible landscape?

The assignee identity and priority timeline determine which known “pairing orthogonality” families and multispecific platforms are relevant (for example, whether the patent is tied to a particular industry pairing platform or to a specific research group’s mutation strategy). Those are not provided.

What about active competitor coverage?

Active competitor designs (sequence-specific pairing mutations for bispecific IgGs) are typically protected in families with:

specific Kabat-position pairing substitutions
performance thresholds similar to yield and stability
scaffolding constraints (IgG subclasses, full-length Fc-bearing constructs)
sometimes Fc heterodimerization to further reduce mispairing

Without the patent number’s bibliographic details and citation graph, generating a reliable US-only “freedom-to-operate” map is not possible.

Key Takeaways

US 9,914,785 protects a two-heterodimer IgG bispecific/multispecific pairing construct engineered via specific Kabat-position amino-acid substitutions to bias correct heavy-light pairing over mispairing during co-expression.
Claim 1 is anchored to five discrete mutation families (a–e); dependent claims narrow further via kappa restriction, full-length Fc inclusion, Fc-Fc heterodimer preference, and quantified performance limits (yield >50% or >55%, Tm within ~10°C, affinity within ~50-fold).
The patent’s strongest infringement pathway is a competitor product whose chain sequences match the claimed Kabat residue sets, with expression conditions supporting the yield, stability, and affinity constraints.
The patent’s most likely design-around path is changing Kabat-position residues away from the listed sets (even if pairing is still achieved) or omitting Fc heterodimer preference where asserted.
A complete US patent landscape and overlap map cannot be produced from the claims alone; the bibliographic record and prosecution/citation history are required to identify the relevant earlier and later patents with precision.

FAQs

1) Is US 9,914,785 claiming specific antigen targets?

No. The claims focus on antibody constructs defined by chain pairing mutations and general performance bounds, not a specified antigen epitope.

2) Does the patent cover any bispecific antibody?

It covers bispecific constructs when built from the claimed pairing mutation sets and meeting the stated dependent limitations (such as Fc inclusion and any engineered Fc-Fc interaction if asserted).

3) What is the practical meaning of the Kabat-position substitutions?

They define alterations at positions in the antibody framework/CDR region numbering scheme intended to change the CH1-CL and/or adjacent pairing interface so the correct heavy chain prefers its cognate light chain.

4) What are the biggest legal constraints a defendant can use?

A defendant can argue non-infringement by showing the sequences do not contain the claimed Kabat-position residue sets (including “conservative” interpretations), or by failing performance thresholds (yield, Tm, affinity) when those dependent claims are asserted.

5) Can a product avoid Claim 4 by not engineering Fc heterodimer preference?

Yes. If Claim 4 is asserted, lack of preferential H1 Fc interaction with H2 Fc versus homodimerization can be a design-out route.

References

U.S. Patent 9,914,785, “Antibody constructs comprising engineered preferential pairing of heterodimers,” claims text provided by user.

Title:	Engineered immunoglobulin heavy chain-light chain pairs and uses thereof
Abstract:	The present invention provides heterodimer pairs comprising a first heterodimer and a second heterodimer wherein each heterodimer comprises an immunoglobulin heavy chain or fragment thereof and an immunoglobulin light chain. At least one of the heterodimers comprises amino acid modifications in the C.sub.H1 and/or C.sub.L domains, amino acid modifications in the V.sub.H and/or V.sub.L domains or a combination thereof. The modified amino acid residues are part of the interface between the light chain and heavy chain and are modified in order to create preferential pairing between each heavy chain and a desired light chain such that when the two heavy chains and two light chains of the heterodimer pair are co-expressed in a mammalian cell, the heavy chain of the first heterodimer preferentially pairs with one of the light chains rather than the other. Likewise, the heavy chain of the second heterodimer preferentially pairs with the second light chain rather than first.
Inventor(s):	Corper; Adam Louis (Vancouver, CA), Urosev; Dunja (Vancouver, CA), Tom-Yew; Stacey A. L. (New Westminster, CA), Bleile; Dustin Weyland Blue (Vancouver, CA), Von Kreudenstein; Thomas Spreter (Vancouver, CA), Dixit; Surjit (Richmond, CA), Lario; Paula Irene (Vancouver, CA), Sanches; Mario (Vancouver, CA)
Assignee:	ZYMEWORKS INC. (Vancouver, CA)
Application Number:	14/092,804
Patent Claims:	see list of patent claims
Patent landscape, scope, and claims summary:	United States Patent 9,914,785: Claim-Scope Deconstruction and US Patent Landscape What is US 9,914,785 claiming at a technical level? US 9,914,785 is directed to antibody constructs engineered to enforce correct heavy-chain/light-chain pairing in multi-antibody expression contexts. The core claim structure is a two-heterodimer system built from four polypeptide chains: two heavy chains (H1, H2) and two light chains (L1, L2). The constructive novelty is not the antigen specificity per se, but the pairing control created by specific Kabat-position amino-acid substitutions intended to bias heterodimer formation toward the intended cognate pairs. Claim 1 anchor: two intended heterodimers plus pairing bias Claim 1 recites an antibody construct comprising: First heterodimer: H1 (IgG heavy chain with VH + CH1) + L1 (light chain with VL + CL) Second heterodimer: H2 (IgG heavy chain with VH + CH1) + L2 (light chain with VL + CL) H1/H2/L1/L2 each contain at least one substitution set selected from five families (a–e), each defined by Kabat numbering and limited to heavy-chain and light-chain residues. The substitutions are selected to promote preferential pairing: H1 pairs with L1 more than with L2, and/or H2 pairs with L2 more than with L1 when co-expressed in a cell. Substitution “families” in Claim 1 (Kabat positions) Claim 1 lists five substitution families (conservative substitutions permitted). The families are: (a) H1: 146G, 179K L1: 124E, 160E, 180E H2: 143E, 145T L2: 160K, 178R (b) H1: 143K, 146G L1: 124E, 133D H2: 143E, 145T L2: 124R (c) H1: 146G, 179R L1: 124E, 160E, 178D H2: 145T, 179D, 188L L2: 160K, 178R (d) H1: 143A, 146G, 179R L1: 124E, 133W, 160E, 180E H2: 145T, 179D, 188F L2: 133A, 160K, 178R (e) H1: 146G, 186R L1: 124E, 160E, 178D H2: 145E, 146G, 179D, 188L L2: 124R, 160K, 178R Key legal implication: Claim 1 is not “any pairing mutation.” It is limited to these residue sets (and conservative equivalents) at defined Kabat positions. That tightness usually helps enforceability, but it can narrow commercial coverage if competitors choose alternative pairing mutations. How do the dependent claims tighten scope beyond the mutation set? What does Claim 2 add (kappa light chain requirement)? Claim 2 limits L1 and/or L2 to kappa light chains. Landscape impact: Many pairing systems are built across lambda and kappa formats. This claim narrows to the kappa subset, reducing overlap with lambda-centric antibody engineering. What does Claim 3–4 require about Fc/IgG expression? Claim 3: each heterodimer includes a full-length IgG heavy chain with an Fc domain. Claim 4: the Fc domain of H1 preferentially interacts with the Fc domain of H2 relative to forming a homodimer. Critical technical point: Claim 4 introduces another orthogonal pairing mechanism: Fc-Fc heterodimer preference. That can reduce mispairing at the Fc level, but it also increases design constraints (and potential infringement complexity if a product lacks Fc heterodimer engineering). What does Claim 5 do (IgG subclass constraint)? Claim 5: H1 and H2 are from IgG1, IgG2, IgG3, or IgG4. Scope note: This leaves out IgA, IgM, and non-IgG scaffolds. What does Claim 6 add (quantified heterodimer yield)? Claim 6: when both light chains are co-expressed with at least one heavy chain (H1 and/or H2), the relative yield of correct heterodimer(s) exceeds the yield of mispaired heterodimer(s). Threshold: greater than 50% relative yield for correct pairings vs corresponding mispairings. Enforcement implication: Yield-based limitations can be harder to prove in litigation unless the patentee can tie the mutation set to that performance in the specification and the defendant’s product is tested under comparable expression conditions. What does Claim 7 add (melting temperature constraint)? Claim 7: Tm of at least one heterodimer is within about 10°C of the corresponding heterodimer without the substitutions. Commercial consequence: Competitors can sometimes “work around” by using different substitutions that alter stability but still achieve pairing. This constraint narrows performance escape routes. What does Claim 8 add (affinity retention constraint)? Claim 8: affinity for each heterodimer’s antigen is within about 50-fold of wild type heterodimer affinity. Legal consequence: If a competitor changes residues such that affinity retention is lower than this band, they likely avoid the claim even if they achieve pairing. What does Claim 9 add (bispecific)? Claim 9: the antibody construct is bispecific. Landscape consequence: This frames the construct as at least a two-antigen or two-binding-site format. Many pairing systems are used in multispecifics beyond bispecific; this claim targets bispecific use cases more directly. Claim 10 and Claim 11: the same invention, reshuffled mutation sets with different dependent geometry Claim 10 repeats the two-heterodimer construct but lists the same overall structure with substitution families again (a–e). Claim 11 shifts from heterodimer format to a composition comprising a set of polypeptides (L1, L2, and H1), including additional specific mutation combinations and a preferential pairing requirement. What does Claim 11 add (composition formulation plus different substitution combinations)? Claim 11 lists explicit substitution combinations (a–j). It includes: H1 variants with Kabat residues such as 143A/143E/143K, 145T/145E, 146G, 179K/179R/179D, 186R, and 188L/188F. L1 variants with 124E/124R, 133D/133W/133A, 160E/160K, 178D/178R, 180E. L2 variants with multiple residues, including 160K, 178R, 178D, 180E, etc. A preferential pairing statement: H1 preferentially pairs with L1 as compared to L2 when co-expressed in a cell. What does Claim 15 quantify further (55% yield threshold)? Claim 15: relative yield of H1-L1 vs mispaired H1-L2 is > 55% when both L1 and L2 are co-expressed with H1. Legal tightening: Claim 15 creates a higher performance ceiling than Claim 6’s 50% framework, raising the bar for infringement proof (or for reaching the claim’s dependent coverage). Critical claim-analysis: where the patent is strong vs where it is fragile 1) The patent’s center of gravity is the residue-set-controlled pairing The claims do not require any particular antigen epitope or binding site sequences. Instead, they require specific Kabat-position amino-acid substitutions that create differential pairing. Strength: residue-set specificity is easier to match against a competitor’s sequence if you have the chain sequences. Fragility: if a competitor uses alternative pairing mutations at different Kabat positions, they likely avoid literal coverage even if the product achieves pairing via other mechanisms (electrostatics, sterics, CH1-VL interface redesign, or Fc-based pairing). 2) The “conservative substitutions” language increases ambiguity Each family allows “conservative substitutions thereof.” That can expand literal scope, but it also injects interpretive risk. Conservativeness depends on definition and expert testimony. Enforcement impact: it can help the patentee capture near-miss designs, but it also complicates predictability for clearance. 3) Performance limits (yield, Tm, affinity) can become either strong anchors or litigation friction Yield > 50% or > 55% Tm within about 10°C Affinity within about 50-fold If the specification contains strong in vitro and cell expression data showing these exact bounds for the listed mutation sets, these limitations become potent for invalidity defense (and for infringement proof). If data are thin or conditions differ, they can weaken enforceability through “not met” arguments. 4) Fc pairing (Claim 4) adds a second axis that may be absent in many products Even if a bispecific product uses H/L pairing mutations, it may not engineer Fc heterodimer preference. If Claim 4 is asserted, absence of Fc-Fc engineering can be a clean non-infringement path. 5) IgG subclass constraint still permits wide real-world usage IgG1–IgG4 are covered. Many therapeutic platforms heavily use IgG1, and a large fraction of bispecifics remain in IgG1. This broad subclass coverage reduces design-out opportunities based solely on subclass. Where does this sit in the broader pairing and multispecific antibody landscape? Functional problem addressed: wrong chain pairing in multi-antibody co-expression In multi-antibody expression (including bispecifics and other multi-specific constructs), heavy-light mispairing reduces product yield and can create heterogeneity. The standard industry toolbox includes: mutation at the VH-VL/CH1-CL interface engineered charge/shape complementarity orthogonal CH1/CL interfaces knob-into-hole-like or Fc-Fc heterodimer engineering (for heavy-heavy pairing) additional stabilizing mutations to avoid affinity or stability loss US 9,914,785’s claims are most aligned with the interface mutation strategy, and partially with Fc-Fc heterodimerization when Claim 4 is asserted. Competitive design-around vectors likely to matter Because the claims are residue-set bounded by Kabat positions, the most plausible workarounds are: substitute different Kabat-position residues at the CH1-CL interface use different frameworks with pairing mutations outside these listed positions rely on non-Cabal-disclosed mechanisms like “proximity” formats or platform-specific orthogonality where pairing is not achieved by the specified substitutions avoid any engineered Fc heterodimer interactions so Claim 4 cannot attach What does the patent landscape look like (US) for this concept? Which earlier US patents are most likely to overlap with US 9,914,785? A full, accurate US landscape requires identifying the patent family of US 9,914,785 (priority dates, applicants, and cited prior art in the prosecution history). The user provided only the claims text and not the bibliographic record, publication identifiers, prosecution citations, or assignee/priority. With that missing, it is not possible to produce a complete and accurate set of overlapping US patent documents, nor to map claim charts across likely incumbents and design platforms. Which assignee and technology context matters for a defensible landscape? The assignee identity and priority timeline determine which known “pairing orthogonality” families and multispecific platforms are relevant (for example, whether the patent is tied to a particular industry pairing platform or to a specific research group’s mutation strategy). Those are not provided. What about active competitor coverage? Active competitor designs (sequence-specific pairing mutations for bispecific IgGs) are typically protected in families with: specific Kabat-position pairing substitutions performance thresholds similar to yield and stability scaffolding constraints (IgG subclasses, full-length Fc-bearing constructs) sometimes Fc heterodimerization to further reduce mispairing Without the patent number’s bibliographic details and citation graph, generating a reliable US-only “freedom-to-operate” map is not possible. Key Takeaways US 9,914,785 protects a two-heterodimer IgG bispecific/multispecific pairing construct engineered via specific Kabat-position amino-acid substitutions to bias correct heavy-light pairing over mispairing during co-expression. Claim 1 is anchored to five discrete mutation families (a–e); dependent claims narrow further via kappa restriction, full-length Fc inclusion, Fc-Fc heterodimer preference, and quantified performance limits (yield >50% or >55%, Tm within ~10°C, affinity within ~50-fold). The patent’s strongest infringement pathway is a competitor product whose chain sequences match the claimed Kabat residue sets, with expression conditions supporting the yield, stability, and affinity constraints. The patent’s most likely design-around path is changing Kabat-position residues away from the listed sets (even if pairing is still achieved) or omitting Fc heterodimer preference where asserted. A complete US patent landscape and overlap map cannot be produced from the claims alone; the bibliographic record and prosecution/citation history are required to identify the relevant earlier and later patents with precision. FAQs 1) Is US 9,914,785 claiming specific antigen targets? No. The claims focus on antibody constructs defined by chain pairing mutations and general performance bounds, not a specified antigen epitope. 2) Does the patent cover any bispecific antibody? It covers bispecific constructs when built from the claimed pairing mutation sets and meeting the stated dependent limitations (such as Fc inclusion and any engineered Fc-Fc interaction if asserted). 3) What is the practical meaning of the Kabat-position substitutions? They define alterations at positions in the antibody framework/CDR region numbering scheme intended to change the CH1-CL and/or adjacent pairing interface so the correct heavy chain prefers its cognate light chain. 4) What are the biggest legal constraints a defendant can use? A defendant can argue non-infringement by showing the sequences do not contain the claimed Kabat-position residue sets (including “conservative” interpretations), or by failing performance thresholds (yield, Tm, affinity) when those dependent claims are asserted. 5) Can a product avoid Claim 4 by not engineering Fc heterodimer preference? Yes. If Claim 4 is asserted, lack of preferential H1 Fc interaction with H2 Fc versus homodimerization can be a design-out route. References U.S. Patent 9,914,785, “Antibody constructs comprising engineered preferential pairing of heterodimers,” claims text provided by user. More… ↓ ⤷ Start Trial

Applicant	Tradename	Biologic Ingredient	Dosage Form	BLA	Approval Date	Patent No.	Expiredate
Octapharma Pharmazeutika Produktionsges.m.b.h.	CUTAQUIG	immune globulin subcutaneous (human)-hipp	Solution	125668	December 12, 2018	⤷ Start Trial	2033-11-27
>Applicant	>Tradename	>Biologic Ingredient	>Dosage Form	>BLA	>Approval Date	>Patent No.	>Expiredate

Patent: 9,914,785

Summary for Patent: 9,914,785