RevMab

anti-CPS1 (human), Rabbit Monoclonal (RM395)

CHF 459.00
In stock
REV-31-1281-00-R100100 µlCHF 459.00
More Information
Product Details
Synonyms Carbamoyl-phosphate Synthase 1; CPSase1
Product Type Recombinant Antibody
Properties
Clone RM395
Isotype Rabbit IgG
Source/Host Rabbit
Immunogen/Antigen A peptide corresponding to Human CPS1.
Application

Immunohistochemistry (IHC): 1:100-1:200 dilution
Western Blot (WB): 1:5000-1:10000 dilution

Crossreactivity Human
Specificity

This antibody reacts to human CPS1.

Purity Protein A purified.
Purity Detail Protein A affinity purified from an animal origin-free culture supernatant.
Concentration N/A
Formulation Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide.
Isotype Negative Control

Rabbit IgG

Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Accession Number P31327
Declaration Manufactured by RevMab Biosciences.
Shipping and Handling
Shipping BLUE ICE
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF
Description

Carbamoyl phosphate synthetase I (CPS1 or CPSI) is a ligase enzyme located in the mitochondria involved in the production of urea. It transfers an ammonia molecule from glutamine or glutamate to a molecule of bicarbonate that has been phosphorylated by a molecule of ATP. The resulting carbamate is then phosphorylated with another molecule of ATP. The resulting molecule of carbamoyl phosphate leaves the enzyme. This reaction is the first committed step of the urea cycle, which is important in the removal of excess urea from cells. Mutations in this gene have been associated with carbamoyl phosphate synthetase 1 deficiency (CPS1D), susceptibility to persistent pulmonary hypertension and susceptibility to venoocclusive disease after bone marrow transplantation.

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