JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB162519

Recombinant Human S2P protein

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant Human S2P protein is a Human Full Length protein, in the 1 to 519 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

S2P, MBTPS2, Membrane-bound transcription factor site-2 protease, Endopeptidase S2P, Sterol regulatory element-binding proteins intramembrane protease, SREBPs intramembrane protease

1 Images
SDS-PAGE - Recombinant Human S2P protein (AB162519)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human S2P protein (AB162519)

ab162519 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, ELISA

applications

Biologically active

No

Accession

O43462

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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

storage-buffer

style
left-column

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>" } } }
style
left-column
style
left-column

Sequence info

[{"sequence":"MIPVSLVVVVVGGWTVVYLTDLVLKSSVYFKHSYEDWLENNGLSISPFHIRWQTAVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSYSSSSSSSSSSSSSSSSSSSSSSSLHNEQVLQVVVPGINLPVNQLTYFFTAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSFPVRAYKRLDGSTECCNNHSLTDVCFSYRNNFNKRLHTCLPARKAVEATQVCRTNKDCKKSSSSSFCIIPSLETHTRLIKVKHPPQIDMLYVGHPLHLHYTVSITSFIPRFNFLSIDLPVVVETFVKYLISLSGALAIVNAVPCFALDGQWILNSFLDATLTSVIGDNDVKDLIGFFILLGGSVLLAANVTLGLWMVTAR","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":519,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"O43462","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
style
left-column

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
style
left-column

Supplementary information

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

S2P also known as Site-2 protease or IMP1 is an intramembrane zinc metalloprotease with a mass around 52 kDa. It carries out the proteolytic cleavage of membrane-bound transcription factors. S2P resides in cellular locations like the endoplasmic reticulum membrane and is highly expressed in tissues such as the liver and muscle. This protease acts after the initial cleavage by Site-1 protease (S1P) playing an important role in regulated intramembrane proteolysis.
Biological function summary

S2P cleaves specific substrates involved in lipid metabolism and stress response. This protease is an integral component of the sterol-regulatory element-binding proteins (SREBPs) complex. The cleavage by S2P releases the active form of SREBPs which translocates into the nucleus to regulate genes responsible for cholesterol and fatty acid synthesis. S2P ensures that these transcription factors maintain lipid homeostasis and adapt to cellular environment changes.

Pathways

S2P significantly influences cholesterol biosynthesis and unfolded protein response pathways. In the cholesterol biosynthesis pathway it regulates the activation of SREBPs which in turn controls cholesterol and lipid biosynthesis genes. Additionally in the unfolded protein response pathway it interacts with proteins such as ATF6 to help manage endoplasmic reticulum stress. These interactions highlight S2P's pivotal role in maintaining cellular balance under varying conditions.

S2P dysfunction can lead to conditions like hypercholesterolemia and metabolic syndrome. Impaired S2P activity disrupts normal cholesterol regulation potentially causing elevated cholesterol levels and related cardiovascular diseases. S2P also connects to ATF6 in response to stress and any disturbances might influence metabolic pathways contributing to metabolic syndrome. Understanding the role of S2P in these diseases offers insights into potential therapeutic approaches for managing lipid-related disorders.
style
left-column

Specifications

Form

Liquid

style
left-column

General info

Function

Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed : 10805775, PubMed : 11163209). Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 : cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached (PubMed : 10805775, PubMed : 27380894, PubMed : 9659902). Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription (PubMed : 10805775, PubMed : 27380894, PubMed : 9659902). Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B) (PubMed : 11163209). Involved in intramembrane proteolysis during bone formation (PubMed : 27380894). In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression (PubMed : 16417584).

Sequence similarities

Belongs to the peptidase M50A family.

style
left-column

Product protocols

style
left-column

Target data

Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed : 10805775, PubMed : 11163209). Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 : cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached (PubMed : 10805775, PubMed : 27380894, PubMed : 9659902). Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription (PubMed : 10805775, PubMed : 27380894, PubMed : 9659902). Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B) (PubMed : 11163209). Involved in intramembrane proteolysis during bone formation (PubMed : 27380894). In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression (PubMed : 16417584).
See full target information MBTPS2
style
left-column
style
left-column
style
right-column

Complementary Products

Proteins & Peptides

AB159808

Recombinant Human ZAN protein

SDS-PAGE - Recombinant Human ZAN protein (AB159808)

  • 0
  • 0
Proteins & Peptides

AB159886

Recombinant Human ZP2 protein

SDS-PAGE - Recombinant Human ZP2 protein (AB159886)

  • 0
  • 0
Proteins & Peptides

AB161249

Recombinant Human VAX1 protein

SDS-PAGE - Recombinant Human VAX1 protein (AB161249)

  • 0
  • 0
Proteins & Peptides

AB163077

Recombinant Human VNN3 protein

SDS-PAGE - Recombinant Human VNN3 protein (AB163077)

  • 0
  • 0

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com