What technology was used to isolate this PDZ domain?

The PDZ domain that binds the beta1-adrenergic receptor was isolated from the library using Yeast Two-hybrid technology. PDZ domains are modular protein-interaction domains specialized for binding to short peptide motifs at the extreme carboxy (C) termini of other proteins.

What is the affinity of this scaffold for its target?

After affinity maturation, PDZ domain variants were identified having affinities (KD=50 nM) for the beta1-adrenergic receptor. This affinity was determined by biosensor technology, confirming its potential for use in various research applications like diagnostic and therapeutic studies.

PDZ domain scaffold protein anti-Human β1-adrenergic receptor

CAT#: SPD-L174

The PDZ domain that bound β1-adrenergic receptor was isolated from the library using Yeast Two-hybrid techonology. PDZ domains are modular protein-interaction domains that are specialized for binding to short peptide motifs at the extreme carboxy (C) termini of other proteins, athough they can also have other modes of interaction. After affinity maturation, PDZ domain variants were identified having affinities (KD=50 nM) for β1-adrenergic receptor as determined by biosensor technology. It's potential to be used in diagnostic, research and therapeutic applications.

Gene Expression

Subcellular Location Figure 1 IF staining of human cell line A-431

Immunofluorescent staining of human cell line A-431 shows localization to cytosol.

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/75322/1717_B5_18_cr57f50e3c439a5_selected.jpg

Normal Tissue Figure 2 IHC staining of human pancreas

Immunohistochemical staining of human pancreas shows strong cytoplasmic positivity in exocrine glandular cells.

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/3431/ihc_selected.jpg

Normal Tissue Figure 3 Colon

Glandular cells Staining: Low Intensity: Weak Quantity:>75% Location: Cytoplasmic/ membranous

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/3431/11306_A_8_3.jpg

Normal Tissue Figure 4 Liver

Cholangiocytes Staining: Low Intensity: Weak Quantity:>75% Location: Cytoplasmic/ membranous

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/3431/11306_A_8_4.jpg

Normal Tissue Figure 5 Kidney

Cells in tubules Staining: Low Intensity: Weak Quantity:>75% Location: Cytoplasmic/ membranous

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/3431/11306_A_8_5.jpg

Normal Tissue Figure 6 Testis

Cells in seminiferous ducts Staining: Low Intensity: Weak Quantity: 75%-25% Location: Cytoplasmic/ membranous

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/3431/11306_A_6_6.jpg

Normal Tissue Figure 7 Cervix

Glandular cells Staining: Medium Intensity: Moderate Quantity:>75% Location: Cytoplasmic/ membranous

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/3431/11306_B_7_3.jpg

RNA Expression Figure 8 RNA cell line category: Cell line enhanced (hTCEpi, hTERT-HME1, PC-3)

Cell lines ordered by descending RNA expression order.

* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/ENSG00000169252-ADRB2

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Specifications

Scaffold Name
PDZ domain

Origin
PSD-95 protein

Core Structure
β-sheet

Target
β1-adrenergic receptor

Species Reactivity
Human

Expression Host
E. coli

Affinity Constant
50 nM

Applications
ELISA; IHC; Microscopy; FC; WB; FuncS

Target

Alternative Names
PSD-95 protein; PDZ domain; BAR; B2AR; ADRBR; ADRB2R; BETA2AR

Gene ID
154

UniProt ID
P07550

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Breast cancer biomarkers at key points during disease progression

Robust Receptor Interaction

We required a scaffold protein capable of interacting with the human beta1-adrenergic receptor for our modular protein-interaction studies. This PDZ domain variant performed well, exhibiting the specialized binding to short peptide motifs we anticipated.

Verified Nanomolar Affinity

Using biosensor technology, we tested the affinity maturation results of this product. The data aligned perfectly with the stated KD of 50 nM, making it a reliable tool for our research into G protein-coupled receptor superfamily signaling complexes.

Q&As

What technology was used to isolate this PDZ domain?

A: The PDZ domain that binds the beta1-adrenergic receptor was isolated from the library using Yeast Two-hybrid technology. PDZ domains are modular protein-interaction domains specialized for binding to short peptide motifs at the extreme carboxy (C) termini of other proteins.
What is the affinity of this scaffold for its target?

A: After affinity maturation, PDZ domain variants were identified having affinities (KD=50 nM) for the beta1-adrenergic receptor. This affinity was determined by biosensor technology, confirming its potential for use in various research applications like diagnostic and therapeutic studies.

View the frequently asked questions answered by Creative Biolabs Support.

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Downloadable Resources

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Datasheet

Datasheet - SPD-L174.pdf

MSDS

MSDS - SPD-L174.pdf

COA

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