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AB113400

Recombinant Human SDSL protein

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Recombinant Human SDSL protein is a Human Full Length protein, in the 1 to 329 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Serine dehydratase-like, Cancerous serine dehydratase, Glutamate racemase, L-serine deaminase, L-serine dehydratase/L-threonine deaminase, L-threonine dehydratase, Serine dehydratase 2, cSDH, SDHL, TDH, SDH 2, SDSL

1 Images
SDS-PAGE - Recombinant Human SDSL protein (AB113400)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human SDSL protein (AB113400)

15% SDS-PAGE of SDSL protein : (1) MW ladder, (2) protein loaded 3ug

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q96GA7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.04% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSHMDGPVAEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQMGSHMDGPVAEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHELKAVLRTPPGALVLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEGCLPPSLTSVVVIVCGGNNINSRELQALKTHLGQV","proteinLength":"Full Length","predictedMolecularWeight":"37.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":329,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96GA7","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The serine dehydratase-like protein (SDSL) also known by its alternate name as serine dehydratase-like 2 exhibits a molecular mass of approximately 42 kDa. SDSL functions mechanically by catalyzing the dehydration reaction of L-serine to form pyruvate and ammonia. This protein is expressed predominantly in the liver with detectable expression in other tissues including the kidney and intestine. Researchers have noted that SDSL might play a role in amino acid metabolism due to its catalytic activity.
Biological function summary

The serine dehydratase-like protein contributes to the metabolism of amino acids an essential process for cellular function and energy production. SDSL does not appear to form part of a larger protein complex but works independently in biochemical pathways related to the breakdown of serine. This activity is significant for maintaining amino acid homeostasis within the cell and supporting gluconeogenesis.

Pathways

Amino acid metabolism and gluconeogenesis represent major biological pathways involving SDSL. In the amino acid metabolism pathway SDSL interacts with enzymes like alanine transaminase and aspartate aminotransferase which further process the products of the dehydratase reaction. In gluconeogenesis the pyruvate produced serves as a substrate for enzymes like pyruvate carboxylase illustrating how SDSL indirectly supports glucose synthesis during fasting or low-carbohydrate intake.

Disturbances in serine metabolism where SDSL is an active participant have connections to disorders such as non-alcoholic fatty liver disease (NAFLD) and phenylketonuria (PKU). In NAFLD an overexpression or aberrant activity of SDSL could contribute to altered amino acid handling influencing liver fat accumulation processes. In PKU connections with phenylalanine hydroxylase show that altered serine metabolism might impact phenylalanine processing indicating a potential area for therapeutic exploration.

Specifications

Form

Liquid

Additional notes

Conventional chromatography techniques (anion exchange followed by gel filtration with 20mM Tris pH 7.5, 2mM EDTA).

General info

Function

Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha-ketobutyrate and pyruvate, respectively (PubMed : 16580895, PubMed : 18342636). Also exhibits racemase activity towards L-glutamate and D-glutamate (By similarity).

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Product protocols

Target data

Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha-ketobutyrate and pyruvate, respectively (PubMed : 16580895, PubMed : 18342636). Also exhibits racemase activity towards L-glutamate and D-glutamate (By similarity).
See full target information SDSL

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