Vector Labs Ab05166-1.1 Anti-C-terminal telopeptide of the α2(I) chain of human collagen I [AbAb01-alpha2Ct], Mouse IgG1, kappa (100 μg) Centrifuge Bundle Savings at Sycamore Life Sciences

Description

Product Class: Purified
Clone ID: AbAb01-alpha2Ct
Synonyms: Collagen alpha-2(VIII) chain; Endothelial collagen
Amount: 100 μg
Application Codes Clone: WB; blocking; inhibition; SPR; IHC; in vivo
Shipping Temperature: Wet Ice
Buffer Composition: PBS with 0.02% Proclin 300.
Original Format: IgA
Storage Temperature: Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement: This reformatted mouse antibody was made using the variable domain sequences of the original Mouse IgA format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement: The original antibody is specific for the C-terminal telopeptide of the α2(I) chain of human collagen I.
Application Notes: The original format of the antibody specifically recognized C-terminal telopeptide of the α2(I) chain of human collagen I, as determined by Western blot assays. The presence of the original format of the antibody decreased the rate of cleavage of procollagen chains in a concentration-dependent fashion. The original format of the antibody blocked telopeptide-mediated collagen/collagen interactions reducing the amount of collagen fibrils accumulated in vitro and in keloid-like organotypic constructs (Chung et al., 2008; PMID: 18650436). The human IgG1 and F(ab')2 formats of the antibody recognized C-terminal telopeptide of the α2(I) chain of human collagen by western blot analysis. The binding affinity of the mIgA, hIgG1 and hF(ab')2 fragments to procollagen I was measured by surface plasmon resonance (Kd= 0.2 nM, 3.2 nM and 2.8 nM respectively). The hIgG1 format of the antibody inhibited fibril formation in vitro. The hIgG1 format of the antibody inhibited the formation of collagen deposits in cell layers. The mIgA format of the antibody immunostained human skin sample, while the hIgG1 version immunostained mouse skin and thymus (Fertala et al., 2013; PMID: 23586407). The scFv format of the antibody bound exclusively to the pro-α2 chain by western blot analysis. The binding affinity of the scFv fragment to procollagen I was measured by surface plasmon resonance (KD = 75 nM). The scFv format of the antibody completely inhibited the formation of collagen fibril at scFv:collagen molar ratio of 16:1 or resulted in the formation of a mixed population of collagen assemblies at ratio 4:1. The scFv fragment primarily interacted with collagen fibrils at the boundaries of a gap region in which the scFv's epitope, i.e. the α2Ct. The scFv variant of the antibody blocked the deposition of collagen fibrils in the gap region existing between cells isolated from tendon and tendon sheath without altering the ability of cells to proliferate and migrate into the border region (Fertala et al., 2014; PMID: 24195607). The original antibody was employed in a in vivo clinically relevant arthrofibrosis model to study its broad mechanisms (Steplewski et al., 2021; PMID: 34492074).

Product Class:	Purified
Clone ID:	AbAb01-alpha2Ct
Synonyms:	Collagen alpha-2(VIII) chain; Endothelial collagen
Amount:	100 μg
Application Codes Clone:	WB; blocking; inhibition; SPR; IHC; in vivo
Shipping Temperature:	Wet Ice
Buffer Composition:	PBS with 0.02% Proclin 300.
Original Format:	IgA
Storage Temperature:	Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement:	This reformatted mouse antibody was made using the variable domain sequences of the original Mouse IgA format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement:	The original antibody is specific for the C-terminal telopeptide of the α2(I) chain of human collagen I.
Application Notes:	The original format of the antibody specifically recognized C-terminal telopeptide of the α2(I) chain of human collagen I, as determined by Western blot assays. The presence of the original format of the antibody decreased the rate of cleavage of procollagen chains in a concentration-dependent fashion. The original format of the antibody blocked telopeptide-mediated collagen/collagen interactions reducing the amount of collagen fibrils accumulated in vitro and in keloid-like organotypic constructs (Chung et al., 2008; PMID: 18650436). The human IgG1 and F(ab')2 formats of the antibody recognized C-terminal telopeptide of the α2(I) chain of human collagen by western blot analysis. The binding affinity of the mIgA, hIgG1 and hF(ab')2 fragments to procollagen I was measured by surface plasmon resonance (Kd= 0.2 nM, 3.2 nM and 2.8 nM respectively). The hIgG1 format of the antibody inhibited fibril formation in vitro. The hIgG1 format of the antibody inhibited the formation of collagen deposits in cell layers. The mIgA format of the antibody immunostained human skin sample, while the hIgG1 version immunostained mouse skin and thymus (Fertala et al., 2013; PMID: 23586407). The scFv format of the antibody bound exclusively to the pro-α2 chain by western blot analysis. The binding affinity of the scFv fragment to procollagen I was measured by surface plasmon resonance (KD = 75 nM). The scFv format of the antibody completely inhibited the formation of collagen fibril at scFv:collagen molar ratio of 16:1 or resulted in the formation of a mixed population of collagen assemblies at ratio 4:1. The scFv fragment primarily interacted with collagen fibrils at the boundaries of a gap region in which the scFv's epitope, i.e. the α2Ct. The scFv variant of the antibody blocked the deposition of collagen fibrils in the gap region existing between cells isolated from tendon and tendon sheath without altering the ability of cells to proliferate and migrate into the border region (Fertala et al., 2014; PMID: 24195607). The original antibody was employed in a in vivo clinically relevant arthrofibrosis model to study its broad mechanisms (Steplewski et al., 2021; PMID: 34492074).

Specifications

More Information
Brand	Vector Labs
UNSPSC	12161500

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