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AB127522

Recombinant Human IZUMO1 protein (His-DHFR tag N-Terminus)

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(1 Publication)

Recombinant Human IZUMO1 protein (His-DHFR tag N-Terminus) is a Human Fragment protein, in the 51 to 211 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

Izumo sperm-egg fusion protein 1, Oocyte binding/fusion factor, Sperm-specific protein izumo, OBF, IZUMO1

Key facts

Purity

>95%

Expression system

Escherichia coli

Tags

His-DHFR tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q8IYV9

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.58% Sodium chloride, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"18.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":211,"aminoAcidStart":51,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q8IYV9","tags":[{"tag":"His-DHFR","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

IZUMO1 also known as Immunoglobulin superfamily member 9 is a protein important to the process of fertilization. IZUMO1 has a molecular mass of approximately 37 kDa. It localizes specifically to the acrosomal region of sperm cells. This protein plays a mechanical role in sperm-egg fusion an essential step for successful fertilization allowing sperm cells to recognize and bind to the egg cell membrane. Expression of IZUMO1 is limited to mature sperm assuring its involvement exclusively during fertilization.
Biological function summary

The protein acts when spermatozoa interact with oocytes. IZUMO1 facilitates the binding through forming a complex with Juno the receptor on the egg surface. This interaction is necessary for the initial contact and fusion between the sperm and egg membranes. The IZUMO1-Juno pairing ensures proper docking and fusion enabling the combination of genetic materials from both gametes. The specificity of this binding prevents cross-species fertilization maintaining species integrity during reproduction.

Pathways

IZUMO1 has involvement in the fertilization pathway. It works directly in the sperm's fusion process an important part of the reproductive process. IZUMO1 interacts closely with other sperm proteins such as CD9 which play roles in adhesion and fusion events. These pathways incorporate IZUMO1 within the larger reproductive framework where it functions alongside these proteins to ensure successful gamete fusion and genetic transfer.

IZUMO1's functionality connects to issues of infertility. Defects or deficiencies in IZUMO1 expression or function can lead to male infertility due to ineffective sperm-egg fusion. Additionally fertility research identifies Juno as a complementary protein in this context as abnormalities in either protein may disrupt fertilization processes and contribute to reproductive challenges. Understanding IZUMO1 offers insight into diagnostic and therapeutic possibilities for treating infertility cases where sperm-egg membrane fusion is compromised.

Specifications

Form

Lyophilized

Additional notes

>95% by SDS Page

General info

Function

Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1 : IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Acts a ligand for the human-specific oolemma epitope FCRL3/MAIA during fertilization (PubMed : 36070373). FCRL3/MAIA replaces IZUMO1R/JUNO as IZUMO1 receptor after sperm-egg adhesion, which permits species-specific gamete fusion (PubMed : 36070373). Plays a critical role in sperm-oolemma binding prior to plasma membrane fusion. Can mediate cell-cell fusion in cultured mammalian cells independently of its binding to IZUMO1R/JUNO (By similarity).

Sequence similarities

Belongs to the Izumo family.

Post-translational modifications

N-glycosylated. Glycosylation is not essential for fusion and for proper protein trafficking in sperm.. Phosphorylated. The cytoplasmic C-terminus is phosphorylated and undergoes phosphorylation changes during epididymal transit.

Product protocols

Target data

Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1 : IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Acts a ligand for the human-specific oolemma epitope FCRL3/MAIA during fertilization (PubMed : 36070373). FCRL3/MAIA replaces IZUMO1R/JUNO as IZUMO1 receptor after sperm-egg adhesion, which permits species-specific gamete fusion (PubMed : 36070373). Plays a critical role in sperm-oolemma binding prior to plasma membrane fusion. Can mediate cell-cell fusion in cultured mammalian cells independently of its binding to IZUMO1R/JUNO (By similarity).
See full target information IZUMO1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

International journal of biological sciences 19:2234-2255 PubMed37151878

2023

Cytochalasin D restores nuclear size acting on F-actin and IZUMO1 localization in low-quality spermatozoa.

Applications

Unspecified application

Species

Unspecified reactive species

Guillaume Martinez,Donato Cappetta,Marialucia Telesca,Konrad Urbanek,Giuseppe Castaldo,Magali Dhellemmes,Vincenza Grazia Mele,Teresa Chioccarelli,Veronica Porreca,Anne-Laure Barbotin,Angèle Boursier,Florian Guillou,Charles Coutton,Sophie Brouillet,Antonella De Angelis,Liberato Berrino,Riccardo Pierantoni,Gilda Cobellis,Rosanna Chianese,Francesco Manfrevola
View all publications

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