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AB163753

Recombinant Human FAM111A protein (GST tag N-Terminus)

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Recombinant Human FAM111A protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 611 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

KIAA1895, FAM111A, Serine protease FAM111A

1 Images
SDS-PAGE - Recombinant Human FAM111A protein (GST tag N-Terminus) (AB163753)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human FAM111A protein (GST tag N-Terminus) (AB163753)

ab163753 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q96PZ2

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Complementary Products

Primary Antibodies

AB184572

Anti-FAM111A antibody [EPR14407]

RabMAb|Recombinant

Immunocytochemistry/ Immunofluorescence - Anti-FAM111A antibody [EPR14407] (AB184572)

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Proteins & Peptides

AB163926

Recombinant Human SPATS2 protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human SPATS2 protein (GST tag N-Terminus) (AB163926)

  • 0
  • 0
Proteins & Peptides

AB163795

Recombinant Human ERAP2 protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human ERAP2 protein (GST tag N-Terminus) (AB163795)

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  • 0
Proteins & Peptides

AB164034

Recombinant Human GCC1 protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human GCC1 protein (GST tag N-Terminus) (AB164034)

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  • 0
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Reactivity data

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

[{"sequence":"MSCKKQRSRKHSVNEKCNMKIEHYFSPVSKEQQNNCSTSLMRMESRGDPRATTNTQAQRFHSPKKNPEDQTMPQNRTIYVTLKVNHRRNQDMKLKLTHSENSSLYMALNTLQAVRKEIETHQGQEMLVRGTEGIKEYINLGMPLSCFPEGGQVVITFSQSKSKQKEDNHIFGRQDKASTECVKFYIHAIGIGKCKRRIVKCGKLHKKGRKLCVYAFKGETIKDALCKDGRFLSFLENDDWKLIENNDTILESTQPVDELEGRYFQVEVEKRMVPSAAASQNPESEKRNTCVLREQIVAQYPSLKRESEKIIENFKKKMKVKNGETLFELHRTTFGKVTKNSSSIKVVKLLVRLSDSVGYLFWDSATTGYATCFVFKGLFILTCRHVIDSIVGDGIEPSKWATIIGQCVRVTFGYEELKDKETNYFFVEPWFEIHNEELDYAVLKLKENGQQVPMELYNGITPVPLSGLIHIIGHPYGEKKQIDACAVIPQGQRAKKCQERVQSKKAESPEYVHMYTQRSFQKIVHNPDVITYDTEFFFGASGSPVFDSKGSLVAMHAAGFAYTYQNETRSIIEFGSTMESILLDIKQRHKPWYEEVFVNQQDVEMMSDEDL","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":611,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q96PZ2","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

FAM111A also known as Family with Sequence Similarity 111 Member A is a protein with a molecular mass of approximately 66 kDa. It is expressed in various tissues including the spleen thymus and liver. FAM111A possesses a serine protease domain which links it to protease activity. Its expression is especially noted in actively proliferating cells suggesting a function in cell cycle regulation.
Biological function summary

FAM111A participates in DNA replication and cell division. It often associates with components of the DNA replication machinery acting to maintain genomic stability during the cell cycle. Researchers have identified FAM111A as an essential factor for proper DNA synthesis. The protein may also interact with other cellular factors to ensure accurate DNA replication although it does not appear to form part of a large stable complex.

Pathways

Studies connect FAM111A to the DNA replication and repair pathways. It interacts with proteins involved in maintaining the integrity of the genome such as those in the replication fork machinery. FAM111A participates alongside proteins like DNA polymerase and helicase where it contributes to their regulation and function. This involvement places FAM111A as an important component for effective DNA damage response and repair.

Mutations in FAM111A are linked to Kenny-Caffey Syndrome and Gracile Bone Dysplasia. These relate to abnormal growth and skeletal development. The protein's dysfunction disrupts normal cell cycle and growth regulator mechanisms. Alterations affecting FAM111A may also involve interactions with cyclins or cyclin-dependent kinases important for proper cell cycle progression. Understanding FAM111A's role can provide insights into therapeutic approaches for managing these conditions.
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Specifications

Form

Liquid

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General info

Function

Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed : 32165630). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed : 32165630). Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors (PubMed : 32165630). Required for PCNA loading on replication sites (PubMed : 24561620). Promotes S-phase entry and DNA synthesis (PubMed : 24561620). Acts also as a restriction factor for some viruses including SV40 polyomavirus and vaccinia virus (PubMed : 23093934, PubMed : 37607234). Mechanistically, affects nuclear barrier function during viral replication by mediating the disruption of the nuclear pore complex (NPC) via its protease activity (PubMed : 33369867, PubMed : 37607234). In turn, interacts with vaccinia virus DNA-binding protein OPG079 in the cytoplasm and promotes its degradation without the need of its protease activity but through autophagy (PubMed : 37607234).

Sequence similarities

Belongs to the FAM111 family.

Post-translational modifications

Autocatalytically cleaved; activating the protein (PubMed:32165630). Autocatalytic cleavage takes place in trans (PubMed:32165630).

Subcellular localisation

Nucleus

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Product protocols

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Target data

Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed : 32165630). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed : 32165630). Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors (PubMed : 32165630). Required for PCNA loading on replication sites (PubMed : 24561620). Promotes S-phase entry and DNA synthesis (PubMed : 24561620). Acts also as a restriction factor for some viruses including SV40 polyomavirus and vaccinia virus (PubMed : 23093934, PubMed : 37607234). Mechanistically, affects nuclear barrier function during viral replication by mediating the disruption of the nuclear pore complex (NPC) via its protease activity (PubMed : 33369867, PubMed : 37607234). In turn, interacts with vaccinia virus DNA-binding protein OPG079 in the cytoplasm and promotes its degradation without the need of its protease activity but through autophagy (PubMed : 37607234).
See full target information FAM111A
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